Use of 1,3-selective lipases for pitch control in pulp and paper processes

Abstract

Formulations for pitch control, and methods of making and using thereof, are described herein. The formulations contains one or more 1,3-selective lipases. 1,3-selective lipases catalyze the hydrolysis of the terminal ester groups in triglycerides leaving the internal ester group intact. The enzyme formulations can contain one or more additives, such as dispersants, metal ions, absorbents, adsorbents, cationic polymers, and combinations thereof. The enzyme formulation is typically applied as a solution to the pulp stock. The enzyme formulations can be applied at any of one or more various points during the pulping and paper manufacturing processes. The use of selective lipase(s) decreases the total concentration of fatty acids in the system, and catalyzes the formation of monoglycerides, which are more effective at dispersing fatty acids than glycerol, the product of non-selective lipases, thereby improving pulp and paper machine runnability and pulp and paper quality.

1 . A method for controlling pitch in the production of pulp or paper, the method comprising contacting the pulp with an enzyme composition comprising one or more 1,3-selective lipases. 
     
     
         2 . The method  claim 1 , wherein the one or more 1,3-selective lipases, are isolated from one or more bacteria selected from the group consisting of  Rhiopus oryzae, Rhizopus delemar, Rhizopus arrhhizus, Rhizopus niveus, Aspergillus niger, Pseudomonas alcaligenes, Pseudomonas fragi, Pseudomonas cepacia, Mucor miehei, Humicola lanuginosa, Penicillum roqueforti, Chromobacterium viscosum, Candida cylindracea , and  Candida rugosa.    
     
     
         3 . The method of  claim 1 , wherein the one or more 1,3-selective lipases are isolated from an organism that has been genetically engineered to express or overexpress the one or more 1,3-selective lipases. 
     
     
         4 . The method of  claim 1 , wherein the dosage of the lipase(s) is from about 0.02-10 lbs/ton of oven dried pulp. 
     
     
         5 . The method of  claim 4 , wherein the dosage of the lipase(s) is from about 0.02-5 lbs/ton of oven dried pulp. 
     
     
         6 . The method of  claim 4 , wherein the dosage of the lipase(s) is from about 0.1-3 lbs/ton of oven dried pulp. 
     
     
         7 . The method of  claim 1 , wherein the method further comprises contacting the pulp with one or more dispersants, surfactants, absorbents, adsorbents, or combinations thereof. 
     
     
         8 . The method of  claim 7 , wherein the one or more dispersants, surfactants, absorbents, adsorbents, and combinations thereof are contact with the pulp at the same time as the enzyme composition or at a different time than the enzyme composition. 
     
     
         9 . The method of  claim 7 , wherein the dispersant is selected from the group consisting of primary and branched alkoxylates, fatty acid alkoxylates, phosphate esters and their alkoxylates, alkylphenol alkoxylates, block copolymers of ethylene and propylene oxide, alkanesulfonates, olefinsulfonates, fatty amine alkoxylates, glyceride alkoxylates, glycerol ester alkoxylates, sorbitan ester alkoxylates, polyethylene glycol esters, polyalkylene glycols, polyacrylic acids, sodium polyacrylate, acrylic acid copolymer, acrylate copolymer, acrylic crosslinked copolymer, and their derivatives; maleic acid and acrylic acid or acrylate copolymer, maleic acid/olefin copolymer, and their derivatives, polyvinyl alcohol/polyvinyl acetate copolymers, polyvinyl pyrrolidone and copolymers thereof, and combinations thereof. 
     
     
         10 . The method of  claim 9  wherein the concentration of the dispersant is from about 0.002 to about 10 kilograms/ton of pulp. 
     
     
         11 . The method of  claim 10  wherein the concentration of the dispersant is from about 0.004 to about 3 kilograms/ton of pulp. 
     
     
         12 . The method of  claim 9  where the polyvinyl pyrrolidone and copolymers thereof have a molecular weight between 7,000 to 2,500,000 daltons, more preferably between 400,000 and 2,000,000. 
     
     
         13 . The method of  claim 9  wherein the polyvinyl alcohol/polyvinyl acetate copolymers have a molecular weight between 5,000 and 500,000 daltons, more preferably between 50,000 and 150,000, and a hydrolysis degree between 50% and 100%, more preferably between 70% and 95%. 
     
     
         14 . The method of  claim 1 , wherein the enzyme formulation further comprises one or more polycationic substances which modify the activity of the one or more 1,3-selective lipases. 
     
     
         15 . The method of  claim 14 , wherein the one or more polycationic substances are selected from the group consisting of aluminum sulfate, sodium aluminate, poly(aluminum chloride), polyethyleneimine (PEI), poly-DADMAC, polyvinylpyrrolidone (PVP). 
     
     
         16 . The method of  claim 1 , wherein the pulp stock is produced by a process selected from the group consisting of mechanical pulping, semichemical pulping, chemi-thermomechanical pulping, bleached Kraft pulping and recovered fiber pulping. 
     
     
         17 . The method of  claim 16  wherein the pulp is a mechanical pulp selected from the group consisting of groundwood pulp, pressurized groundwood pulp and thermomechanical pulp. 
     
     
         18 . The method of  claim 1 , wherein the pulp is derived from virgin fibers, recycled fibers, and combinations thereof. 
     
     
         19 . The method of  claim 18 , wherein the recycled fibers are selected from the group consisting of old corrugated containers (OCC), old newsprint (ONP), mixed office waster (MOW), old magazines (OMG), and combinations thereof. 
     
     
         20 . The method of  claim 1 , wherein the pulp is contacted with the enzymes at a location in the pulping process selected from the group consisting of the latency chest, reject refiner chest, disk filter or decker feed or accept, TMP whitewater system; the low density (“LD”) chest, the medium density or consistency chest (MC), the high density (“HD”) chest, the decker, the blend chest; the machine chest; the headbox, the paper machine (“PM”), the white water system, and combinations thereof. 
     
     
         21 . The method of  claim 1 , wherein the formulation is maintained in the pulp stock at a temperature of about 10° C. to about 95° C. 
     
     
         22 . The method of  claim 21  wherein the formulation is maintained in the pulp stock at a temperature of about 30° C. to about 75° C. 
     
     
         23 . The method of  claim 1 , wherein the pulp is contacted with the enzyme formulation at a pH from about 3 to about 11. 
     
     
         24 . The method of  claim 23 , wherein the pulp is contacted with the enzyme formulation at a pH from about 4 to about 7.5. 
     
     
         25 . An enzyme composition used in the method of  claim 1 , the composition comprising one or more 1,3-selective lipases. 
     
     
         26 . The composition of  claim 25 , wherein the one or more 1,3-selective lipases, are isolated from one or more bacteria selected from the group consisting of  Rhizopus oryzae, Rhizopus delemar, Rhizopus arrhhizus, Rhizopus niveus, Aspergillus niger, Pseudomonas alcaligenes, Pseudomonas fragi, Pseudomonas cepacia, Mucor miehei, Humicola lanuginosa, Penicillum roqueforti, Chromobacterium viscosun, Candida cylindracea , and  Candida rugosa.    
     
     
         27 . The composition of  claim 26 , wherein the one or more 1,3-selective lipases are isolated from an organism that has been genetically engineered to express or overexpress the one or more 1,3-selective lipases. 
     
     
         28 . The composition of  claim 25 , wherein the composition further comprises one or more dispersants, surfactants, absorbents, adsorbents, or combinations thereof. 
     
     
         29 . The composition of  claim 28 , wherein the dispersant is selected from the group consisting of primary and branched alkoxylates, fatty acid alkoxylates, phosphate esters and their alkoxylates, alkylphenol alkoxylates, block copolymers of ethylene and propylene oxide, alkanesulfonates, olefinsulfonates, fatty amine alkoxylates, glyceride alkoxylates, glycerol ester alkoxylates, sorbitan ester alkoxylates, polyethylene glycol esters, polyalkylene glycols, polyacrylic acids, sodium polyacrylate, acrylic acid copolymer, acrylate copolymer, acrylic crosslinked copolymer, and their derivatives; maleic acid and acrylic acid or acrylate copolymer, maleic acid/olefin copolymer, and their derivatives, polyvinyl alcohol/polyvinyl acetate copolymers, polyvinyl pyrrolidone and copolymers thereof, and combinations thereof. 
     
     
         30 . The composition of  claim 25 , wherein the enzyme composition further comprises one or more polycationic substances which modify the activity of the one or more 1,3-selective lipases. 
     
     
         31 . The composition of  claim 30 , wherein the one or more polycationic substances are selected from the group consisting of aluminum sulfate, sodium aluminate, poly(aluminum chloride), polyethyleneimine (PEI), poly-DADMAC, polyvinylpyrrolidone (PVP). 
     
     
         32 . A kit containing the composition of  claim 23  and at least one container. 
     
     
         33 . The kit of  claim 32 , further comprising instructions for administering the enzyme composition. 
     
     
         34 . The kit of  claim 32 , further containing one or more additives selected from the group consisting of dispersants, surfactants, absorbents, adsorbents, or combinations thereof. 
     
     
         35 . The kit of  claim 34 , wherein the one or more additives are in the same container as the enzyme composition. 
     
     
         36 . The kit of  claim 34 , wherein the one or more additives are in one or more different containers than the enzyme composition.