WO1994029522A1 - Paper strengthened with solubilized collagen, and method for making the same - Google Patents
Paper strengthened with solubilized collagen, and method for making the same Download PDFInfo
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- WO1994029522A1 WO1994029522A1 PCT/US1994/006040 US9406040W WO9429522A1 WO 1994029522 A1 WO1994029522 A1 WO 1994029522A1 US 9406040 W US9406040 W US 9406040W WO 9429522 A1 WO9429522 A1 WO 9429522A1
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- collagen
- slurry
- pulp
- solubilized
- insoluble
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
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- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21H—PULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
- D21H17/00—Non-fibrous material added to the pulp, characterised by its constitution; Paper-impregnating material characterised by its constitution
- D21H17/20—Macromolecular organic compounds
- D21H17/21—Macromolecular organic compounds of natural origin; Derivatives thereof
- D21H17/22—Proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21H—PULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
- D21H11/00—Pulp or paper, comprising cellulose or lignocellulose fibres of natural origin only
- D21H11/14—Secondary fibres
-
- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21H—PULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
- D21H21/00—Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties
- D21H21/14—Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties characterised by function or properties in or on the paper
- D21H21/18—Reinforcing agents
Definitions
- Paper strengthened with solubilized collagen and method for making the same.
- This invention relates to a process for making solubilized collagen and for making solubilized collagen-strengthened paper that 5 provides advantages over other known processes that make improved papers.
- the invention also relates to the improved solubilized collagen and improved paper made by the process.
- the invention has utility in making low cost solubilized collagen and in binders for cellulosic products, especially in the production of recycled 10 cellulosic paper that has improved mechanical properties and low cost.
- Skin is composed of four distinct layers, which are, proceeding from outside-in: (1) a thin outer layer of epithelium termed the "epidermis", which is rich in the protein keratin, not collagen;
- hides may merely be “cured” in salt and/or other biocidal solutions to stop microbial degradation
- many hides that are intended for use in leather manufacture are "limed", that is, soaked in a saturated solution of hydrated lime (calcium hydroxide) and water.
- the liming process initiates the loosening of the epidermis and the subcutaneous layer, and is the first step in the dehairing process. After liming is complete, the hair, epidermis, and any residual flesh, fat and surface muscles are removed by mechanical scraping, and the dermal layer is mechanically cut, along with enough of the corium layer to give the final leather its required thickness, from the remaining inner corium layer.
- the primary interest is on the dense collagen- rich dermal layer, which is about 25% of the thickness of the corium layer.
- the dermal tissue receives separate chemical and tanning treatments to stabilize the collagen structure.
- the residual portion of the corium layer that is separated from the dermal layer is termed the "limed split" and is a by-product waste of the leather manufacturing process. It is these limed splits that become, for example, the collagen-rich feedstock for sausage casing production, and that have been used as the source of collagen for the examples herein.
- the skin imbibes and binds water, and becomes highly swollen; in the process it acquires a very alkaline pH of about 12.5.
- the chemistry of the liming process is quite well understood.
- the skins Prior to further leather processing, and in the collagen production process considered here, the skins must be "delimed” by soaking in acid or salt solutions.
- recycled cellulosic materials are preferably used to replace end products where virgin cellulosic materials have historically been used.
- products made from recycled cellulosic materials usually have physical characteristics that differ from those made from virgin materials. One of these important characteristics is strength which is often significantly reduced.
- a French journal article by G. Sauret et al Le collagne ans la fabrication du papier, Revue A.T.P.I., Vol 33, No. 8, Octobre 1979, pp 374-365, discloses a mechanical method using a Turmix-Waring blender for preparing collagen.
- the mechanically treated collagen is insoluble. It is combined with cellulose pulp and made into paper sheets.
- the present invention uses a method that combines small amounts of soluble collagen with cellulosic material as further described herein.
- a typical embodiment of the invention is a method for producing an aqueous solution of solubilized collagen by the steps of (a) providing an aqueous ground slurry of insoluble collagen and adjusting the pH of the slurry to obtain activity for a later added proteolytic enzyme; (b) adding the proteolytic enzyme to the pH adjusted slurry; (c) reacting the slurry and enzyme of step b and ⁇ or recycled insoluble collagen and enzyme of step e at a temperature, T, and for a time, t, effective for forming a solution increased in solubilized collagen; (d) adding additional water and insoluble collagen to the solution of step (c) and mixing; (e) separating at least some of the solution of step d containing solubilized collagen from the insoluble collagen, whereby at least a portion of the insoluble collagen and proteolytic enzyme is recycled to step c, and a separated solution containing solubilized collagen is withdrawn as product.
- step c may be repeated two, three, four or more times. Additional enzyme may be added to the recycled insoluble collagen from step e that substantially replaces enzyme removed with the withdrawal of product or when the rate of reaction on recycling decreases below a predetermined level.
- the method is operated as a continuous process.
- the reaction may typically be stopped by adjusting the pH to that where the proteolytic enzyme is substantially inactive; and/or by reducing the temperature to that where the proteolytic enzyme is substantially inactive.
- the liquid or solids content of the wet ground slurry is preferably adjusted so that the solids are at a concentration of about 0.1 to about 1.0 wt %; in step c the temperature, T, is preferably about 5°C to about 30°C, and more preferably about 15°C to about 28°C.
- the solids concentration is between about 0.3 to 0.35 wt % and the reaction of step c is at a temperature of about 10 to about 30°C, and for a time of 10 to 72 hours; more preferably the temperature is between 15°C and 28°C.
- Typical proteolytic enzymes are selected from the group consisting of porcine mucosal pepsin, bro elain, chymopapain, chymotrypsin, collagenase, ficin, papain, peptidase, proteinase A, proteinase K, trypsin, icrobial protease, and combinations of such enzymes. More preferably the proteolytic enzyme is pepsin or a microbial acid protease.
- the pH is preferably about 1.5 - 3.0, and the temperature about 15°C to about 28°C.
- at least 80 wt % of the insoluble collagen is converted to soluble collagen with a number average molecular weight 300,000 daltons and above; while more preferably at least 90 wt % of the insoluble collagen is converted to soluble collagen and the number average molecular weight is above 1,000,000 daltons.
- a further typical embodiment of the invention includes a method for producing an aqueous solution of solubilized collagen by the steps of (a) providing an aqueous ground slurry of insoluble collagen; (b) adjusting the water or solid content of the wet ground slurry whereby the insoluble collagen is at a concentration that promotes substantially maximum solubilized collagen concentration in a final product; (c) adjusting the pH of the slurry from step b to obtain activity for a proteolytic enzyme added in step d; (d) adding and mixing the proteolytic enzyme with the pH adjusted slurry; (e) reacting the slurry of step d and ⁇ or the recycled insoluble collagen of step g at a temperature, T, and for a time, t, effective for forming a solution comprising solubilized collagen derived from the insoluble collagen particles; (f) adding additional water and insoluble collagen to the solution containing solubilized collagen in step e and mixing; (g) separating at least some of the solution of step f containing solub
- step e may be repeated two, three, four or more times. Additional enzyme may be added to the recycled insoluble collagen from step e that substantially replaces enzyme removed with the withdrawal of product or when the rate of reaction on recycling decreases below a predetermined level.
- the method is operated as a continuous process. The reaction may typically be stopped by adjusting the pH to that where the proteolytic enzyme is substantially inactive; and/or by reducing the temperature to that where the proteolytic enzyme is substantially inactive.
- the liquid or solids content of the wet ground slurry is preferably adjusted so that the solids are at a concentration of about 0.1 to about 1.0 wt %; in step e the temperature, T, is preferably about 5°C to about 30°C, and more preferably about 15°C to about 28°C. In another preferred embodiment the solids concentration is between about 0.3 to 0.35 wt % and the reaction of step e is at a temperature of about 10 to about 30°C, and for a time of 10 to 72 hours; more preferably the temperature is between 15°C and 28°C.
- Typical proteolytic enzymes are selected from the group consisting of porcine mucosal pepsin, bromelain, chymopapain, chymotrypsin, collagenase, ficin, papain, peptidase, proteinase A, proteinase K, trypsin, microbial protease, and combinations of such enzymes. More preferably the proteolytic enzyme is pepsin or a microbial acid protease.
- porcine mucosal pepsin the pH is preferably about 1.5 - 3.0, and the temperature about 15°C to about 28°C.
- the insoluble collagen is converted to soluble collagen and the number average molecular weight is above 300,000 daltons; while more preferably at least 90 wt % of the insoluble collagen is converted to soluble collagen.
- Another embodiment of the invention is a method for producing an aqueous solution of solubilized collagen by the steps of providing an aqueous ground slurry of insoluble collagen; adjusting the water or solid content of the wet ground slurry whereby the insoluble collagen is at a concentration that promotes substantially maximum solubilized collagen concentration that is adapted to strengthen paper in a final product; adjusting the pH of the slurry from Step b to obtain activity for a proteolytic enzyme added in Step d; adding the proteolytic enzyme to the pH adjusted slurry and reacting at a temperature, T, and for a time, t, effective for forming solubilized collagen from the insoluble collagen particles; controlling the reaction conditions for obtaining a high concentration of soluble collagen by measuring the concentration of solubilized collagen and the molecular weight of the solubilized collagen, whereby the reaction is complete when the number average molecular weight fraction above 300,000 daltons and the concentration are substantially maximized; and withdrawing the aqueous solution of solubilized collagen as
- Feed material for the process can typically come from a variety of sources as long as the feed is relatively clean and has collagen containing material of relatively small particle size, see for example the method of Komanowsky et al discussed below.
- One typical method for preparing the feed material of a wet ground slurry of insoluble collagen from animal tissues includes the steps: (a) providing soft animal tissues containing collagen; (b) cleaning the collagen containing tissues to remove hair, fat, carbohydrates, and other contaminants; (c) cutting the cleaned collagen containing tissues into small pieces; (d) mixing the small pieces with water to obtain a slurry; (e) adjusting the pH of the slurry substantially near the isoelectric point of collagen from the tissues; (f) wet grinding the resulting pH adjusted slurry to obtain a slurry of insoluble collagen.
- the pH of this method is typically about 3 to about 7.
- the invention further encompasses the unique aqueous solutions of solubilized collagen produced by the above methods.
- a yet further embodiment of the invention includes a method for making a collagen strengthened cellulosic sheet by the steps of: (a) providing a cellulosic pulp slurry; (b) adding solubilized collagen to the pulp slurry, and mixing for a time effective for interaction of the cellulosic pulp slurry and solubilized collagen; (c) forming the interacted cellulosic pulp slurry and solubilized collagen into a sheet; and (d) drying the sheet.
- the formed sheet may be a sheet such as paper.
- Another embodiment includes a method for using solubilized collagen for strengthening paper by mixing the solubilized collagen with a cellulosic pulp slurry, molding the mixture and drying.
- a still further embodiment includes a strengthened cellulosic pulp composition of a dried reaction product of a mixture of solubilized collagen and cellulosic pulp.
- Another typical embodiment is a strengthened paper product of paper prepared from a mixture of solubilized collagen and cellulosic pulp.
- Yet another typical embodiment includes a method for making a collagen strengthened cellulosic sheet by the steps of: (a) mixing a cellulosic material selected from the group consisting of virgin paper pulp, broke, reclaimed newsprint, reclaimed carton container, or a mixture thereof with a solution comprising water, or water and caustic, and mechanically pulping until a pulp slurry is formed having a consistency of about 3 wt% to about 6 wt% based on dry pulp solids; (b) diluting the pulp slurry to a consistency of about 1 wt% to about 3 wt% based on dry pulp solids and adjusting pH to about 3.5 to about 7.0; (c) adding between about 0.1 dry wt% to about 2 dry wt% soluble collagen (based on dry weight of cellulosic material) to the diluted pulp slurry, and mixing at a shear rate and a time effective for interaction of the diluted pulp slurry solids and soluble collagen, whereby at least a substantial
- step c diluting the collagen-pulp slurry to between about 0.1 dry wt% and 1 dry wt% consistency; (e) forming the collagen-pulp slurry into a sheet and drying the sheet.
- the pH may be adjusted with an acid selected from the group consisting of muriatic acid, HC1 , HN0 3 , H 2 SO , and acetic acid.
- the method may include the additional step of coating the sheet of step e with sizing prior to drying.
- the sizing further may be a collagen hydrolyzate having a number average molecular weight of 100,000 daltons or less.
- the dried sheet may be calendered.
- the caustic of step a can be a NaOH solution with a concentration of about 0.25 wt% to about 1.00 wt% based on dry weight of cellulosic pulp solids, and a pH range 10-14.
- the solubilized collagen has a number average molecular weight above 300,000 daltons, and most preferably above about 1,000,000 daltons.
- the mixing shear rate and other conditions are adapted to promote collagen-pulp interactions without denaturation of the collagen triple helical structure.
- the collagen-paper slurry preferably has a consistency of about 0.5 dry wt%.
- an alum/rosin additive is added after pulping in step a or after dilution in step b or after refining.
- the formed sheet can be wet pressed to a preselected thickness prior to drying.
- the additional step of refining the pulp/water slurry from Step a is preferred to fibrillate cellulose fibers in order to obtain a selected degree of freeness upon forming a sheet in Step e.
- the degree of freeness is preferably between about 100 CSF and about 150 CSF and when substantially reclaimed carton container is selected the degree of freeness is preferably between about 300 CSF and about 400 CSF.
- a yet further embodiment includes the steps of a method for making a collagen strengthened cellulosic sheet by the steps of: (a) mixing a cellulosic material selected from the group consisting of virgin paper pulp, broke, reclaimed newsprint, reclaimed carton container, or a mixture thereof with a solution comprising water, or water and NaOH, and mechanically pulping until a pulp slurry is formed having a consistency of about 3 wt% to about 6 wt% based on dry pulp solids; (b) diluting the pulp slurry to a consistency of about 1 wt% to about 3 wt% based on dry pulp solids and adjusting pH to about 3.5 to about 7.0; (c) adding an alum/rosin additive to the pulp slurry after Step a or to the diluted pulp slurry after Step b; (d) forming the diluted pulp slurry containing alum rosin into a sheet; (e) coating one or both sides of the sheet with collagen hydrolyzate having a
- Another typical embodiment includes a method for making a collagen strengthened cellulosic sheet by the steps of: (a) mixing a cellulosic material selected from the group consisting of virgin paper pulp, broke, reclaimed newsprint, reclaimed carton container, or a mixture thereof with a solution comprising water, or water and NaOH, and mechanically pulping until a pulp slurry is formed having a consistency of about 3 wt% to about 6 wt% based on dry pulp solids; (b) diluting the pulp slurry to a consistency of about 1 wt% to about 3 wt% based on dry pulp solids and adjusting pH to about 3.5 to about 7.0; (c) providing an aqueous ground slurry of insoluble collagen; (d) adjusting the water or solid content of the wet ground slurry whereby the insoluble collagen is at a concentration that promotes substantially maximum solubilized collagen concentration and molecular weight in a final product; (e) adjusting the pH of the slurry from Step d
- soluble collagen comprising between about 0.1 dry wt% to about 2 dry wt% soluble collagen (based on dry weight of cellulosic material) to the diluted pulp slurry, and mixing at a shear rate and a time effective for interaction of the diluted pulp slurry solids and soluble collagen, whereby at least a substantial portion of the soluble collagen is bound to the paper pulp to form a collagen-pulp slurry; (k) diluting the collagen-pulp slurry to between about 0.1 dry wt% and 1 dry wt% consistency; (1) forming the collagen-pulp slurry into a sheet; and drying the sheet.
- a still further embodiment includes a method for producing a collagen strengthened sheet by the steps of: (a) providing an aqueous ground slurry of insoluble collagen and adjusting the pH of the slurry to obtain activity for a proteolytic enzyme added in Step b; (b) adding the proteolytic enzyme to the pH adjusted slurry;
- Another typical embodiment includes a method for producing an aqueous solution of high molecular weight solubilized collagen by the steps of: (a) providing an aqueous ground slurry of insoluble collagen; (b) adjusting the water or solid content of the wet ground slurry whereby the insoluble collagen is at a concentration that promotes substantially maximum solubilized collagen concentration and molecular weight in a final product; (c) adjusting the pH of the slurry from Step b to obtain activity for a proteolytic enzyme added in Step d; (d) adding and mixing the proteolytic enzyme with the pH adjusted slurry; (e) reacting the slurry of Step d at a temperature, T, and for a time, t, effective for forming a solution comprising high molecular weight solubilized collagen derived from the insoluble collagen particles; (f) adding additional water and insoluble collagen to the solution containing high molecular weight solubilized collagen in Step e and mixing; (g) separating at least some of the solution of Step
- Figure 1A is a plot showing the non-Newtonian behavior of the collagen solutions. Viscosity of diluted solutions of solubilized collagen of the invention (A) and BA-1 collagen solutions (B) at two shear rates (20 and 100 rp ) . Viscosity, in centipoise, is plotted in the ordinate (vertical scale) and the approximate solids concentration, in mg/mL, is plotted in the abscissa (horizontal scale).
- Figure IB is a plot showing the ratio of the viscosity determined at 20 rpm to the viscosity at 100 rpm, termed here the "viscosity ratio".
- the data is calculated from the data in Figure 1A for both solubilized collagen of the invention (A) or the BA-1 collagen solutions (B).
- the viscosity ratio is plotted in the ordinate (vertical scale) and the approximate solids concentration, in mg/mL, is plotted in the abscissa (horizontal scale).
- Figure 2 is a plot of the data for Example 1A showing the viscosity at 20 rpm and 100 rpm. Viscosity, in centipoise, is plotted in the ordinate (vertical scale) and the duration of the reaction, in hours, is plotted in the abscissa (horizontal scale).
- Figure 3 is a plot of a small-scale batch collagen solubilizing reaction demonstrating the pepsin recycle of Example 3A. The viscosity ratio is plotted in the ordinate (vertical scale) and the time of reaction, in hours, is plotted in the abscissa (horizontal scale).
- Figure 4 is a plot of the development of viscosity ratios in Examples 5A (denoted by A) and 6A (denoted by B). The viscosity ratio is plotted in the ordinate (vertical scale) and the time of reaction, in hours, is plotted in the abscissa (horizontal scale).
- solubilized collagen material added to a cellulose pulp prior to the papermaking process (i.e, mixed with the cellulose pulp fibers in the machine chest), resulted in a significant increase in strength of the paper-collagen composite.
- This result is surprising since the prior art teaches that larger insoluble aggregates of collagen, such as those produced by mechanical diminution of bovine hides, are necessary.
- soluble collagen can be expected to thermally denature at the fluids temperatures employed in papermaking (greater than about 40 °C). Denatured collagen is not expected to be as useful as native collagen aggregates.
- Acidified collagen - collagen that has been treated with an acid or extracted by an acid solution.
- Calendering - process of creating surface smoothness and hardness in paper typically by on-line compression between (counter-rotating) cylinders.
- Cellulosic pulp - fibers from cellulosic materials that could be wet or dry and produced by mechanical, chemical or other means.
- Collagen gel - collagen that exists in its native molecular state in a continuous, highly hydrated fibrillar network.
- Collagen sizing - collagen added as a coating after paper sheet has been made.
- Degree of freeness a measure of how easily (freely) water will drain from a paper sheet during production, performed in a standardized test apparatus; one industry recognized standard is Canadian Standard Freeness (CSF).
- CSF Canadian Standard Freeness
- collagen and cellulosic e.g. paper pulp
- mixing is at a relatively lower shear rate (as compared to beating) that is conducive to the reaction of higher molecular weight collagen with cellulosic pulp so as to obtain interaction of solubilized collagen and cellulosic pulp.
- Reclaimed paper - paper as received from recycling operations Reclaimed paper - paper as received from recycling operations.
- Recycled paper - reclaimed paper that has been reprocessed and made into new usable paper Recycled paper - reclaimed paper that has been reprocessed and made into new usable paper.
- Solubilized collagen - collagen that has been treated to separate the collagen fibrils to render them soluble while retaining the normal triple-helical assembly of native collagen; covalent bonds between collagen fibrils are broken so that smaller collagen molecules can go into solution; this is in comparison to mechanically worked and or acid treated collagen that merely makes the collagen pieces physically smaller but does not break the covalent bonds between fibrils; the solubilized collagen used herein has been solubilized by an enzymatic treatment that breaks the covalent bonds between collagen fibrils.
- Viscosity ratio the ratio of two viscosity measurements of a solution at two different shear rates. This is one typical way to follow the increase or decrease of viscosity due to an increase or decrease of solubilized collagen being produced from a slurry of insoluble collagen. Another typical method would be to use only the viscosity measurement to follow the increase or decrease of solubilized collagen.
- One typical embodiment of the first general embodiment achieves lower costs of operation by utilizing recycle steps to recapture and reuse enzyme that would normally be lost on removal of soluble collagen product solutions.
- Another typical embodiment of the first general embodiment also has low costs of operation but does not utilize the recycle steps to recapture enzyme.
- the solubilized collagen is sent directly to its end use, such as in papermaking, with no attempt to remove enzyme or otherwise purify the solubilized collagen.
- Advantages of the first general embodiment of the invention are in: (1) minimizing the cost of preparing soluble collagen by processing directly from ground skin material to the maximum amount of soluble macromolecules; and (2) at the same time, maximizing the degree of conversion to soluble collagen material capable of binding to cellulosic pulp and controlling the molecular weight of the soluble collagen material in order to enhance the binding effect to the pulp fibers, thereby maximizing the resulting tensile strength and/or other mechanical properties of the paper product.
- Another major advantage of using solubilized collagen over the insoluble larger aggregates of the prior art, in the production of cellulosic products such as paper, is greater uniformity in the distribution of collagen in the cellulosic pulp.
- Bovine skin was selected as the collagen source in the examples described here because collagen preparation methods from skin have been widely reported, and the material is a high volume by-product of the major industries of beef production and leather manufacture; however, it is expected that collagen obtained from other sources (e.g. tendon) will work in the process also.
- Collagen solubilization of skin has been accomplished by an enzymatic hydrolysis process with an animal stomach enzyme (e.g. pepsin) and several other enzymes without any other purification steps.
- an animal stomach enzyme e.g. pepsin
- Other (untested) enzymes may yield faster or cheaper conversion of collagen-containing tissues, and the process has not necessarily been optimized to minimize enzyme requirements and production time.
- the process has been scaled to produce approximately 500 gallons of 0.3-0.4% collagen solution, and it has been demonstrated to be relatively easy to control.
- pepsin used was a crude (relatively unpurified) powder from pig stomach mucosa (Cat. No. P7125) purchased from Sigma Chemical Company, St. Louis, M0. Lot # 070H0437 of this product, used in the examples, contains approximately 15% protein (by UV), with an activity of 91 pepsin units/mg solids and 620 units/mg protein. Residual solids in the preparation appear to be a combination of precipitation salts, buffer salts and/or carbohydrates. Crystallized pepsin has a maximum specific activity of about 3500 units/mg protein.
- pepsin crude powder, from Sigma Chemical Company
- AFP 2000 acid fungal protease from a strain of Aspergi l lus niger, from Solvay Enzymes
- Newlase A from a strain of Aspergi l lus niger
- Newlase II from a strain of Rhizopus niveus, from Amano Enzyme U.S.A.
- Quest AP quest acid protease from a strain of Aspergi T lus niger, from Quest International
- EDC-APA an EDC acid protease A
- EDC-APB an EDC acid protease B, from Enzyme Development Corporation.
- the collagen slurry used herein for Examples 1A-6A was prepared from ground limed-splits of bovine skin.
- the collagen was supplied by Teepak's Sandy Run Plant, Columbia, SC.
- a 1974 USDA report by Komanowsky, M., et al "Production of Comminuted Collagen for Novel Applications", J. American Leather Chew. Assoc , 6, 410-422 (1974), describes techniques for pre-sl icing, acidifying and wet-grinding of limed splits to produce five "comminuted" (ground) collagen products, classified by extent of grinding and the resulting particle size and texture.
- Example 7A to 11A unless otherwise provided the enzymatic collagen solubilization was performed as follows.
- the collagen source (either ground whole hides or ground limed splits) ground as described in Example 7A with an 0.06 inch cutting head and in a water slurry was spun at 4°C in a Beckman J2-21 Centrifuge (OA-20 rotor) at 10,000 rpm for 20 minutes to remove excess liquid. This centrifuge provided a ratio of rpm to gravitation force of about 1:1, thus at 10,000 rpm the G forces were about 10,000X gravity.
- the supernatant liquid was removed and the centrifuged solids (7.5 g) were added to a one liter Erlenmeyer flask that contained deionized water (750 mL).
- Viscosity measurements were made by pouring approximately 100 mL of each reaction mixture into a beaker and bringing to room temperature. The viscosity was measured with a Brookfield Synchro-lectric Viscometer model RVT. Measurements were made at 20 rpm and 100 rpm with spindle No. 3. Three readings were taken at each speed and averaged for the calculation of viscosity in centipoise. Aliquots were removed for viscosity measurements at specified times and then returned to their original flasks.
- BA-1 collagen solution
- This product is sometimes found to be slightly gelled upon receipt.
- the BA-1 is produced by an acid- extraction process, not by an enzymatic reaction as practiced in the present invention.
- Fluid viscosities can be conveniently measured by a variety of relatively simple methods, such as the Brookfield Model #RVT Viscometer (#3 Spindle) used with the examples. In this Brookfield system, the force exerted by a fluid upon a disk, which is rotated at constant rotational speed in the fluid, is used to estimate the fluid viscosity. In the collagen solutions described herein, the fluid viscosity will be strongly dependent on the concentration of dissolved collagen, the molecular weight distribution of the soluble collagen and the fluid temperature, and, to a lesser extent, fluid pH and ionic strength.
- the viscosity was determined at two rotational speeds, 20 and 100 rpm.
- the open circles (-0-) and filled circles (- •-) represent data for solubilized collagen of the invention at 20 rpm and at 100 rpm, respectively.
- the open squares (-D-) and the filled squares (- ⁇ -) represent the data for the BA-1 collagen control at 20 rpm and 100 rpm respectively. Both solutions were more viscous at the lower rotational rate, as expected.
- the viscosities of the collagen produced in the examples and BA-1 preparations were substantially different, with the produced collagen solution having a much higher viscosity at lower collagen concentrations and a steeper slope.
- the open circles (- ⁇ -) represent data from the solubilized collagen of the invention and the open squares (- ⁇ -) represent data from the BA-1 collagen solution.
- the viscosity ratio used herein is a measure of the "degree of conversion" of solid collagen materials to soluble collagen molecules, and also a measure of molecular weight, where higher values of the viscosity ratio will correlate with the desired higher number average molecular weights of the dissolved collagen.
- an increase in viscosity ratio is measuring the increase in concentration of soluble collagen since the molecular weight of the material remains the same. In tests of the examples below, changes in the viscosity and viscosity ratio will be measuring changes in concentration.
- the peak soluble collagen content can be measured by chromatographic and electrophoretic techniques.
- analysis of solubilized collagen composition was routinely performed by SDS polyacrylamide gel electrophoresis (PAGE) that used a 3% stacking gel; 6% running gel, following denaturation by boiling with ⁇ -mercaptoethanol . Some irreversible precipitation occurs during the denaturation process. Gels were stained by Coomassie Blue dye and destained in staining buffer only.
- the buffer system in the gel is 0.112 M Tris acetate, pH 6.4.
- PhastGel SDS Buffer Strips that contain, at pH 8.1, 0.2 M Tricine, 0.2 M Tris, and 0.55% SDS were used to run the gels.
- the separation method was from the PhastSystem Separation Technique File No. 130, Table 2.
- Samples were prepared for Gel Electrophoresis by the addition concentrated stock solutions of SDS (20%) and buffers (5 X stock). The final concentrations were 10 mM Tris/HCl (pH 8.0), 1 mM EDTA, 2 - 2.5% SDS, and 0.01% bromophenol blue. Each sample was then heated at 100°C for 5 minutes and approximately l ⁇ L was applied to the gel. In some early experiments, 2-mercaptoethanol (a reducing agent) was added to the sample before heating. The addition of the 2- mercaptoethanol had no effect on the gel pattern.
- 2-mercaptoethanol a reducing agent
- the gel(s) were stained with the Pharmacia Silver Kit.
- the staining method used was from the PhastSystem Silver Kit Instruction Manual , Table 2.
- the Development time and Background Reduction time were doubled for better visibility on the gels.
- the SDS detergent in the gels disperses all non-covalent collagen aggregates leaving only covalently joined molecules.
- the degree to which these molecules migrate on a gel is related to their molecular weights and approximate molecular weights have been assigned to the collagen bands by co-electrophoresis of molecular weight standards on the same gels.
- PAGE analysis of solubilized collagen indicates bands at -100,000 daltons (alpha-collagen), -200,000 daltons (beta- collagen), -300,000 daltons (gama-collagen) , and bands > 300,000 daltons.
- the intensity of the bands is in inverse order of their molecular weights.
- Analysis for soluble or insoluble collagen was typically performed by first measuring the amount of hydroxyproline in the sample, then correlating this concentration with the collagen. Hydroxyproline was measured on 0.1 mL samples that were dried in polypropylene tubes at 125°C. The samples were dissolved in 0.05 mL 4 M sodium hydroxide, capped, and then autoclaved for 30 minutes. Citric acid (0.05 L of a 1.4 M solution) and chlora ine T reagent (1 mL of a solution that contained 1.41 g chloramine T, 10 mL 1- propanol , 10 mL deionized water, and 30 mL of a pH 6 citric acid/acetic acid buffer) were added to each tube which was then incubated for 20 min.
- HPLC High pressure liquid chromatography
- the SDS in the gels disrupts the collagen aggregates so that only the molecular weights of covalently attached molecules can be determined by this method.
- the first eluting peak (Peak 1) contains molecules with number average molecular weights greater than 300,000 daltons as well as molecules with number average molecular weights of approximately 200,000 daltons and approximately 100,000 daltons. The smaller molecules appear to be constituents of larger aggregates that were disrupted by the SDS.
- the second eluting peak (Peak 2) contained molecules with number average molecular weights of approximately 300,000 daltons, approximately 200,000 daltons and approximately 100,000 daltons. The 200,000 dalton and 100,000 dalton molecules appear to be part of 300,000 aggregates that were disrupted by the SDS detergent.
- the third eluting HPLC peak (Peak 3) contains collagen fragments with number average molecular weights less than approximately 100,000.
- EXAMPLE 1A Approximately 15 g of wet Teepak collagen solids were suspended by magnetic stirrer in 750 ml of Columbus, OH tap water at room temperature. The solution pH was adjusted to 2.1 with concentrated hydrochloric acid (HC1) — approximately 65-70 drops. Crude pepsin powder (0.38 g) was then added with stirring into the collagen suspension to initiate the reaction. The suspension was stirred overnight, during which heating of the solution to 26-27°C or higher sometimes occurred due to conduction from the stirrer plate.
- HC1 concentrated hydrochloric acid
- the viscosity of the solution was measured (20 & 100 rpm) periodically during the second day of the reaction until a maximum in the viscosity ratio was achieved, at which time the solution was stabilized by increasing the pH to 3.0-3.5 and/or by placing the solution in the refrigerator. Increasing the pH above 4.0 may initiate irreversible gelation of the collagen solution.
- EXAMPLE 2A EXAMPLE 2A
- the flask was stirred for about 5 minutes to mix the contents and the pH was readjusted with 30 drops of concentrated HC1 , then the stirrer was turned off and the solids were permitted to settle out. After approximately 30 minutes, 750 ml of supernatant, "Day 1" supernatant (Dl), was decanted into another flask, and stirring of both flasks was resumed.
- the Day 1 Supernatant contained some fine collagen particles, but it contained a much lower suspended solids load than the bottom fraction.
- the progression of the hydrolysis reaction is illustrated by the solid lines (-X-) in Figure 3.
- the circles (-G-) show a plot of the progression hydrolysis reaction of the Day 1 supernatant while the squares (-D-) show a plot of the Day 2 supernatant.
- three typical charges of Teepak collagen were hydrolyzed by a single charge of pepsin, although the rate of hydrolysis appears to be decreasing with each cycle. Because the viscosity ratios of both the Day 1 and Day 2 supernatants appeared to increase after they were decanted from the main reactor, it was apparent that some pepsin and insoluble collagen was transported along with the supernatant.
- the pepsin has a higher affinity for solid collagen particles than for soluble collagen, thus most of the enzyme can be recycled several times before it is removed from the system, thereby minimizing the cost of this reagent.
- Preferably better separation of liquid and solids is obtained if the supernatant is separated from the insoluble collagen by centrifugation.
- a steady state in the processing recycle steps is desired. This is achieved by adding additional enzyme after the product removal step, when the rate of reaction in the recycle steps decreases below a predetermined level. Most preferably, additional enzyme is added that just replaces that lost with the removal of product.
- the solution Prior to using the collagen solution made in this example and in Example 6A, described below, the solution was filtered by passing it through a knitted plastic screen with openings approximately 1 x 3 mm, in order to remove a small number of very slowly degrading skin particles. These particles are characteristically the last material to be dissolved by pepsin and can often be found in the 3-5 mm size range. A large sample of these residual particles was filtered from the collagen solution and their dry weight was measured. Based on projecting this sample to the entire batch of collagen solution, it was estimated that more than 95% of the initial solids were solubilized in this process. EXAMPLE 6A
- Example 6A Since the collagen solution in Example 6A was produced at about a 2-3°C higher reaction temperature during the first day than that in Example 5A, the reaction appears to have progressed more rapidly, reaching completion about 4-5 hours sooner. When the pH was adjusted to about 3.0 the final solution appears to have slowed the enzymatic reaction so that little degradation of the soluble product was observed overnight.
- the process is intended to produce nearly complete conversion of beef hides to a collagen solution using an enzymatic hydrolysis reaction. Objectives for the process are production of soluble collagen product at the maximum yield, while conversion costs and fixed capital expenditures are minimized. The process is not intended to produce food or medical-grade soluble collagen, and therefore requirements for production of clean solutions are minimal, and no purification of the soluble collagen is anticipated. No attempt has been made to remove the remnants of the other skin components (fat, proteoglycans, other proteins, salts, etc.), which are present in the ground-split feedstock at concentrations lower than collagen.
- the process will require a series of cutters and grinders to reduce the feedstock limed splits to a shredded material that can be readily converted to soluble collagen.
- the "front end" of the process will likely look similar to the USDA process for producing comminuted collagen.
- the hides may need to be delimed or acidified to remove residual calcium salts or other biocides.
- the ground solids are then mixed with process water (perhaps a reduced-solids Whitewater stream from a paper plant), the pH is titrated to 2.0-2.2, and enzyme is added to begin the solubilization process.
- the soluble solids can be pumped directly to a paper making process and mixed with refined pulp solids or stabilized and stored.
- USDA feed collagen materials were prepared using the method of Komanowsky et al., cited herein, as follows. Two limed splits and one dehaired and limed hide were rolled up and cut to yield 12 inch wide strips. These strips were passed through a strip cutter and then through a rotary knife cutter, An acidic solution was prepared by dissolving 102.15 g of benzoic acid in 1021.5 g of propionic acid. Acidification was carried out in 55 gallon stainless steel tumbling drums by adding 203 lbs of water and 521 g of the above acid solution to the material from the limed hide splits and 235 lb of water and 603 g of acid solution to the whole hide material. The drums were tumbled 15 minutes per hour for four hours.
- USDA ground limed splits were centrifuged at 4°C for 20 minutes at 10,000 rpm. The supernatant liquid was removed and the centrifuged limed splits (15 g) were added to a 2 L Erlenmeyer flask that contained deionized water (1500 mL) . The suspension was stirred with a magnetic stirrer (2 inch stir bar) and the pH was adjusted to pH 2.1 with concentrated hydrochloric acid. Pepsin (0.76 g) was added to the flask, which was then stirred in an incubator set to 18°C. Aliquots of the reactions (100 mL) were removed at different times and analyzed for viscosity (Table 2A) .
- Teepak limed splits were centrifuged at 4°C for 20 minutes at 10,000 rpm. The supernatant liquid was removed and the centrifuged limed splits (35 g) were added to a 4 L Erlenmeyer flask that contained deionized water (3500 mL). The suspension was stirred with a magnetic stirrer (2 inch stir bar) and the pH was adjusted to pH 2.1 with concentrated hydrochloric acid. Pepsin (1.75 g) was added to the flask, which was then stirred in an incubator set to 20.5°C. Aliquots of the reactions (200 mL) were removed at different times and analyzed for viscosity (Table 2A) . The pH of each aliquot was adjusted to between pH 3 and pH 3.5 and the samples were stored at 4°C until they were used to make paper.
- Gel electrophoresis indicates the presence of significant concentrations of approximately 200,000 dalton collagen and approximately 100,000 dalton collagen even after reaction at 30°C for 18.5 hours. Thus, in the absence of detergent there may be significant amounts of 300,000 or higher molecular weight material. Substantial high molecular weight collagen was present as evidenced by the high areas of HPLC peaks 1 and 2 in samples indicated by footnotes c and d.
- Microbial proteases were reacted with ground limed splits from two sources at 17°C .
- a summary of the optimum results with regards to protease concentration and pH is shown in Table 5A.
- Newlase II (0.08 g) 2.6 1840 18
- Collagen solutions prepared by the above examples appear to be stable at room temperature for 12-24 hours, and stability can be enhanced by increasing solution pH to 3.0-3.5 and/or by reducing the solution temperature to 5-10°C.
- the process has demonstrated the feasibility of production of a low-cost soluble collagen product by the substantially complete solubilization of beef hide collagen (ground limed-splits) .
- the process can be conducted at near-ambient conditions and is relatively easy to control.
- Of particular interest is the recycle method that reduces the cost of the relatively expensive proteolytic enzymes.
- the second general embodiment typically utilizes the solubilized collagen produced in the first general embodiment or if desired solubilized collagen can be obtained from other methods.
- One major advantage of using the solubilized collagen of the first general embodiment is of course the low cost of the material so produced. This cost factor is a major advantage in the paper making art.
- the invention improves the strength of recycled paper, conventional paper, and mixtures thereof.
- the invention is especially useful in producing recycled paper because recycled paper made from recycled cellulosic fibers is generally weaker than paper made from virgin cellulose fibers.
- the feedstocks in the invention typically are: virgin paper pulp which is paper pulp made from nonrecycled materials; broke which is scrap at the papermaking plant; reclaimed newsprint which is recycled newspaper and similar paper; reclaimed corrugated container which is recycled old corrugated container and similar material; similar cellulose based papers; and mixtures thereof.
- the invention discloses the use of collagen solubilized with enzymes to improve the strength and other properties of paper type products made from cellulose fibers.
- the method for making a collagen strengthened paper comprises mixing feedstock with water, or water and caustic (e.g. NaOH), and mechanically pulping until a pulp slurry is formed.
- the pulp slurry has a consistency of about 3 to about 6 wt % based on dry pulp solids.
- the pulp slurry is then diluted to a consistency of about 1 to about 3 wt% based on dry pulp solids and adjusted to a pH of about 3.5 to about 7.0.
- solubilized collagen is added to the diluted pulp slurry, and the resulting slurry is mixed at a shear rate and a time effective for interacti on of the di l uted pul p sl urry sol ids and sol ubl e col l agen, whereby a substanti al porti on of the sol ubi l ized col l agen i s bound to the paper pul p to form a col l agen- pulp sl urry .
- the col l agen-pul p sl urry i s then di l uted, preferably to between about 0.1 and 1 dry wt% consi stency, and final ly the col l agen-pul p sl urry i s formed into a sheet and dried .
- the shredded material was pulped in a Tappi disintegrator for 15 minutes.
- the pulp was mixed with additional water and a sheet was formed in a Noble and Wood headbox with a Duotex 162-DD-226 forming fabric.
- the sheet was wet-pressed on the Noble and Wood and then calendered to increase density (blotter paper was used on each side and the gap on the calender rolls was set at 0.76 mils).
- the sheet was dried on a hot plate surface temperature of about 100 °C under tension for 1 minute.
- Collagen hydrolysate (MW ⁇ 2000 daltons) supplied by Secol (Exton, PA) or soluble native collagen (MW > 300,000 daltons) supplied by Gattefosse' Corp.
- the ONP or OCC was shredded and soaked in a 1 percent sodium hydroxide solution overnight.
- the material was pulped in a Tappi disintegrator for 15 minutes.
- the pulp was put in the headbox of the Nobel and Wood, and water at various temperatures (14-17°C or 36- 38°C) was added.
- the pH of the slurry was 7.
- Various amounts of native collagen solution (0.3 % solids) were added.
- the slurry was allowed to settle and stand for 4 to 10 minutes.
- the sheet was formed on a Duotex 162-DD-225 forming fabric.
- the sheet was wet- pressed on the Noble and wood and then calendered to increase density. (Blotter paper was used on each side and the gap on calender rolls was set at .762 mm).
- the sheet was dried on a hot plate for 1 minute.
- the formed sheets were evaluated for basis weight, burst strength, and tensile properties as reported in Table 2B. This table also details the amount of pulp and collagen additive used. Gains of tensile strength were observed in all samples tested, ranging from about 140-350% over the appropriate control without solubilized collagen. While ONP and OCC controls were approximately 25% as strong as the Kraft paper standard, several samples were stronger than the Kraft standard. No correlation was observed between the amount of collagen added and the tensile strength improvement.
- the machine's dryer section consists of two banks of 91 cm diameter dryer cans, seven cans in the first section and five cans in the second section. Between the dryer sections is a size press arrangement which can be operated as a horizontal or a vertical unit. With proper rolls installed, the unit can also be used as a breaker stack. Following the second dryer section is an eight roll, seven nip calender stack. Rolls up to 102 cm in diameter can be wound on the reel.
- Stock from the paper machine chest was pumped via a Fischer- Porter flow controller to the suction side of a fan pump.
- the thick stock was then diluted with white water to operate the stock flow system.
- Production rate on the machine was controlled by the amount of the thick stock flowing into the fan pump.
- the stock was then pumped through an explosion chamber manifold into the primary headbox.
- the headbox was operated under vacuum with a top holey roll.
- Machine speed was approximately 175 ft/min. resulting in a paper throughput of about 300 lbs./hr.
- the forming fabric on the 91 cm Fourdrinier paper machine was a design 463 Monoflex JDL 145 x 120 mesh double layer with: forming Board, three 7.6 cm diameter table rolls, five foil boxes with four foils each, four flat boxes with adjustable vacuum. Paper property (e.g. tensile strength, tear strength, burst strength) improvements obtained from the 1% solubilized collagen additions (Table 4B) .
- machine direction tensile strength improvements were in the range of 25-30% while improvements in the 100% old corrugated containers and old newsprint stocks were in the range of 15-20%.
- MD Machine Direction
- CD Cross Direction
- Tear Tear Strength, grams; Caliper, mm; Mullen Burst, MPa
- BOD Biological Oxygen Demand, mg/liter.
- CD Cross Direction
- Tear Tear Strength, grams; Caliper, mm; Mullen Burst, MPa
- BOD Biological Oxygen Demand, mg/liter.
- Basis weight is the paper weight in kg/279 m 2 (lbs. per 3000 sq.ft.) of paper.
- Example 4B Mixing of Soluble Collagen and Pulp Fiber Prior to Headbox
- Pulp slurries were prepared from ONP and OCC paper stocks at 3% consistency by shredding the materials, soaking them in 1% NaOH overnight, rinsing the soaked solids in tap water, and pulping the rinsed solids in a Tappi disintegrator for 15 minutes.
- the pulp slurry was heated on a hot plate with manual stirring to approximately 120 - 125 °F.
- An aliquot of the heated pulp slurry (183 g) was combined with an aliquot of one of the diluted collagen solutions (63 g), and the combined collagen-pulp slurry was stirred by a blade-type mixer for 15 min.
- the resulting consistency of the pulp in the slurry was about 2.2%.
- the collagen solids to pulp solids ratio for these experiments therefore were approximately 0.5%, 1%, 2% and 4%.
- the initial temperature of the pulp-collagen slurry was approximately 106 °F +/- 3°F (41°C +/- 2°C), and this temperature decreased to approximately 95°F by the end of the stirring period.
- the collagen-pulp slurry was put in the headbox of the Nobel and Wood handsheet system and collected by drainage through a Duotex 162-DD-226 forming fabric.
- the formed sheet was wet pressed, then calendered between blotter paper with the calender gap set at 30 mils. The sheet was then dried on a hot plate under tension for 1 min.
- Handsheets were equilibrated overnight in a controlled environment room (72 °F/50 %RH), then evaluated for basis weight (BW) and tensile strength (TS). Three sheets were prepared and tested for each sample condition. Results are summarized in Table 5B.
- Pulp % (lb/3000 ft 2 ) TS* TS/BW* (%)
- the apparent saturation process observed is interpreted as confirmation that interactions between soluble collagen molecules and pulp fiber surfaces is the predominate mechanism of strength enhancement, as opposed to the directly additive strength enhancement behavior that would be anticipated if these were no interactions between two populations of insoluble fibers mixed int he same proportions.
- the OCC fibers appeared to saturate at a lower collagen-to- pulp-solids ratio than did the ONP fibers.
- the pH of the flasks were adjusted to Proximately 3.5 and the viscosities were measured at 20 rpm.
- the viscosity of the 19 °C reaction was 620 cps and the viscosity of the 32 °C reaction was 10 cps.
- Both collagen preparations were added to pulp (collagen is approximately 1% of pulp) and the ability of these preparations to improve the properties of paper were measured.
- the preparation made at 19 ° provided no tensile strength/basis weight enhancement.
Abstract
Description
Claims
Priority Applications (7)
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JP7501881A JPH08503753A (en) | 1993-06-16 | 1994-05-27 | Paper reinforced with solubilized collagen and method of making same |
BR9405410-0A BR9405410A (en) | 1993-06-16 | 1994-05-27 | Paper reinforced with solubilized collagen, and method for producing the same. |
CA002142621A CA2142621A1 (en) | 1993-06-16 | 1994-05-27 | Paper strengthened with solubilized collagen, and method for making the same |
EP94921919A EP0658227A1 (en) | 1993-06-16 | 1994-05-27 | Paper strengthened with solubilized collagen, and method for making the same |
AU72437/94A AU7243794A (en) | 1993-06-16 | 1994-05-27 | Paper strengthened with solubilized collagen, and method for making the same |
NO950539A NO950539L (en) | 1993-06-16 | 1995-02-14 | Paper reinforced with solubilized collagen, as well as process for making it |
FI950672A FI950672A (en) | 1993-06-16 | 1995-02-15 | Paper reinforced with solubilized collagen and method for its preparation |
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US08/078,932 | 1993-06-16 | ||
US08/078,932 US5316942A (en) | 1993-06-16 | 1993-06-16 | Process for the production of low-cost soluble high-molecular weight collagen |
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CA (1) | CA2142621A1 (en) |
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1993
- 1993-06-16 US US08/078,932 patent/US5316942A/en not_active Expired - Fee Related
-
1994
- 1994-05-27 CA CA002142621A patent/CA2142621A1/en not_active Abandoned
- 1994-05-27 WO PCT/US1994/006040 patent/WO1994029522A1/en not_active Application Discontinuation
- 1994-05-27 JP JP7501881A patent/JPH08503753A/en active Pending
- 1994-05-27 RU RU95107657/12A patent/RU95107657A/en unknown
- 1994-05-27 US US08250803 patent/US5460967B1/en not_active Expired - Fee Related
- 1994-05-27 NZ NZ269003A patent/NZ269003A/en unknown
- 1994-05-27 CN CN94190510.1A patent/CN1112368A/en active Pending
- 1994-05-27 BR BR9405410-0A patent/BR9405410A/en not_active Application Discontinuation
- 1994-05-27 EP EP94921919A patent/EP0658227A1/en not_active Withdrawn
- 1994-05-27 AU AU72437/94A patent/AU7243794A/en not_active Abandoned
- 1994-05-30 TW TW083104898A patent/TW309556B/zh active
-
1995
- 1995-02-15 FI FI950672A patent/FI950672A/en unknown
- 1995-06-07 US US08/488,368 patent/US5686262A/en not_active Expired - Fee Related
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Also Published As
Publication number | Publication date |
---|---|
FI950672A (en) | 1995-03-10 |
US5460967B1 (en) | 1998-03-10 |
TW309556B (en) | 1997-07-01 |
BR9405410A (en) | 1999-09-08 |
CN1112368A (en) | 1995-11-22 |
CA2142621A1 (en) | 1994-12-22 |
NZ269003A (en) | 1996-06-25 |
JPH08503753A (en) | 1996-04-23 |
US5316942A (en) | 1994-05-31 |
US5686262A (en) | 1997-11-11 |
EP0658227A1 (en) | 1995-06-21 |
FI950672A0 (en) | 1995-02-15 |
US5460967A (en) | 1995-10-24 |
RU95107657A (en) | 1996-12-10 |
AU7243794A (en) | 1995-01-03 |
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