Paper making and fiber liberation – Processes of chemical liberation – recovery or purification... – With chemical or physical modification of liberated fiber
Reexamination Certificate
2001-08-29
2003-10-21
Alvo, Steve (Department: 1731)
Paper making and fiber liberation
Processes of chemical liberation, recovery or purification...
With chemical or physical modification of liberated fiber
C162S072000, C435S278000
Reexamination Certificate
active
06635146
ABSTRACT:
BACKGROUND OF THE INVENTION
In the manufacture of paper products, such as facial and bath tissues and paper towels, the wet strength and the dry strength of the product are important properties. To achieve these properties, it is common practice to add certain strengthening agents to an aqueous suspension of the papermaking fibers prior to forming the paper sheet. While effective in achieving targeted strength properties, these chemicals are expensive and may be detrimental for other properties (e.g., bulk) or can cause problems for the papermaking process when the whitewater has to be reused.
Therefore, there is a need for a less expensive and more convenient method of improving the sheet strength properties of papermaking fibers.
SUMMARY OF THE INVENTION
It has now been discovered that certain hydrolytic enzymes can randomly react with the cellulose chains at or near the surface of the papermaking fibers to create single aldehyde groups on the fiber surfaces which are part of the fiber. These aldehyde groups, the reducing ends left after random hydrolysis of &bgr;-1,4 glucosidic bonds in cellulose, become sites for cross-linking with exposed hydroxyl groups of other fibers when the fibers are formed into sheets and dried, thus increasing sheet strength. In addition, by randomly cutting or hydrolyzing the fiber cellulose chains predominantly at or near the surface of the fiber, degradation of the interior of the fiber cell wall is avoided or at least minimized. Consequently, paper or tissue made from these fibers alone, or made from blends of these fibers with untreated pulp fibers, show an increase in strength properties such as dry tensile, wet tensile, tear, z-direction tensile (surface integrity), etc.
Hence, in one aspect, the invention resides in a method for treating papermaking fibers comprising mixing an aqueous suspension of papermaking fibers and one or more hydrolytic enzymes, optionally in the presence of surfactants, optionally in the presence of other non-cellulolytic enzymes or non-hydrolytic chemical reagents, wherein aldehyde groups are formed predominantly at or near the surface of the fibers.
In another aspect, the invention resides in a method for handling the aqueous suspension of aldehyde-rich, enzyme-treated fibers comprising mechanical beating or kneading if desired, and/or mixing with supplemental chemical additives as needed.
In yet another aspect, the invention resides in a method for making a paper sheet comprising: (a) forming an aqueous suspension of papermaking fibers treated with one or more hydrolytic enzymes capable of randomly hydrolyzing cellulose or hemicellulose to create aldehyde groups; (b) feeding the aqueous suspension into a papermaking headbox; (c) depositing the aqueous suspension onto a forming fabric, whereby the fibers are retained on the surface of the forming fabric in the form of a web while water containing the hydrolytic enzyme(s) passes through the fabric; (d) collecting and recycling the water to recombine the hydrolytic enzyme(s) with additional papermaking fibers to form an aqueous suspension; and (e) drying the web to form a paper sheet.
Particular hydrolytic enzymes useful for purposes of this invention are those enzymes which randomly hydrolyze cellulose and/or hemicellulose to create aldehyde groups. Such enzymes include, without limitation, cellulases, hemicellulases, endo-cellulases, endo-hemicellulases, carboxymethylcellulases (“CMCases”) and endo-glucanases. It is known that these enzymes, in particular the cellulases, will degrade the fibrous cell wall, eventually improving pliability, flexibility or softness in coarser webs, but certainly impairing tensile properties at the same time. If these enzymes are not freed of their cellulose binding domain (a step called truncation), they require the presence of a surfactant to moderate the reaction and attain the desired hydrolysis under more controlled conditions. Particularly suitable enzymes for this purpose are truncated endo-glucanases and carboxymethylcellulases, which do not require the presence of a surfactant.
For the purposes of this invention, truncated monocomponent endo-glucanases or truncated carboxymethylcellulases can be advantageous relative to multi-component cellulases because of their purity (in particular, low or no exocellulase activity) and hence greater treatment control resulting in minimal cell wall damage. However, truncated multicomponent cellulases can also work well, since the reactivity of the exo-glucanase portion is severely restricted by chance. A suitable commercially available truncated endo-glucanase is sold by Novozymes North America, Inc. (Franklinton, N.C.), under the name Novozyme® 613, SP 988 or Novozyme® 51016. A related CBD-free CMCase is the commercial preparation EG-40N offered by Clariant Corporation (Charlotte, N.C.). Still, any other hydrolytic enzymes (natural, modified or even an artificial array of peptides) which possess endo-glucanase or carboxymethylcellulase activity can essentially produce similar results.
Suitable papermaking fibers include any virgin or recycled papermaking fibers known in the art, particularly including softwood fibers, such as northern softwood kraft fibers, and hardwood fibers, such as eucalyptus fibers.
As mentioned above, if the hydrolytic enzyme is not truncated, the presence of a surfactant is preferred in the enzyme treatment step for optimal results. A preferred surfactant is a nonionic surfactant, commercially available Tween® 80 (ICI Specialties) or any of the other Tween® 60 series products which are POE sorbitan derivatives. Other suitable nonionoic surfactants include D1600® from High Point Chemical Corp.; D1600® is an alkoxylated fatty acid. Furthermore, aryl alkyl polyetheralcohol, e.g. Union Carbide's Triton® X-100 series of surfactants; alkyl phenyl ether of polyethylene glycol, e.g Union Carbide's Tergitol® series of surfactants; alkylphenolethylene oxide condensation products, e.g. Rhone Poulenc, Incorporated's Igepal® series of surfactants. In some cases an anionic surfactant may be used depending on the type of pulp used. Examples of suitable anionic surfactants are: ammonium or sodium salts of a sulfated ethoxylate derived from a 12 to 14 carbon linear primary alcohol; such as Vista's Alfonic® 1412A or 1412S; and sulfonated naphthalene formaldehyde condensates, e.g. Rohm and Haas's Tamol® SN. In some cases a cationic surfactant can be used, especially when debonding is also desired. Suitable cationic surfactants include imidazole compounds, e.g. Ciba-Geigy's Amasoft® 16-7 and Sapamine® P quaternary ammonium compounds; Quaker Chemicals' Quaker® 2001; and American Cyanamid's Cyanatex®.
The amount of surfactant, if present, can be from about 0.5 to about 6 pounds per metric ton of pulp, more specifically from about 1 to about 5 pounds per metric ton of pulp, more specifically from about 2 to about 4 pounds per metric ton of pulp, and still more specifically from about 2 to about 3 pounds per metric ton of pulp. The specific amount will vary depending upon the particular enzyme being used and the enzyme dosage.
The extent of the hydrolytic modification will depend on the dosage of enzyme applied. The amount of enzyme administered can be denoted in terms of its activity (in enzymatic units) per mass of dry pulp. In general, endo-glucanase activity (“CMCase” activity) in cellulases can be assayed by viscosimetry using carboxymethylcellulose (CMC) as a substrate. The higher the activity in a given enzyme preparation, the more pronounced the decay of viscosity will be after a given reaction (incubation) time under predefined experimental conditions. Novo Nordisk Analytical Method 302.1/1-GB, available on request, can be used to assay endoglucanase activity. It calls for the determination of the viscosity loss of a particular solution of CMC (such as Aqualon 7LFD, initial concentration 34 gpL) after 30 minutes of incubation with a given enzyme preparation at pH 7.5 (phosphate buffer) at 40° C. The method relies on the construction of a c
Lonsky Werner Franz Wilhelm
Negri Alberto Ricardo
Alvo Steve
Croft Gregory E.
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