Lipases from mammals and fishes

Reviews in Fisheries Science

Volumn 17, Issue 1, 2009, Pages 18-40

  Kurtovic, Ivan ^a,b   Marshall, Susan N ^b   Zhao, Xin ^a   Simpson, Benjamin K ^a  

^a MCGILL UNIVERSITY   (Canada)

^b THE NEW ZEALAND INSTITUTE FOR PLANT AND FOOD RESEARCH LIMITED   (New Zealand)

Author keywords

Bile salt; Carboxyl ester lipase (CEL); Fish; Pancreatic lipase (PL); Protein engineering; Triglyceride (TG)

Indexed keywords

AVES; MAMMALIA; PISCES;

EID: 61449155591     PISSN: 10641262     EISSN: 15476553     Source Type: Journal    
DOI: 10.1080/10641260802031322     Document Type: Article

References (201)

1. Abouakil, N., E. Rogalska, J. Bonicel, and D. Lombardo. Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application to the human bile salt-stimulated lipase. Biochim. Biophys. Acta, Lipids LipidMetab., 961: 299-308 (1988).
2. Aires-Barros, M. R., M. A. Taipa, and J. M. S. Cabral. Isolation and purification of lipases, pp. 243-270. In: Lipases-Their Structure, Biochemistry and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
3. Akoh, C., S. Sellappan, L. Fomuso, and V. Yankah. Enzymatic synthesis of structured lipids, pp. 433-460. In: Lipid Biotechnology (T. Kuo, and H. Gardner, Eds.). New York: Marcel Dekker, Inc. (2002).
4. Albro, P. W., R. D. Hall, J. T. Corbett, and J. Schroeder. Activation of nonspecific lipase (EC 3.1.1.-) by bile salts. Biochim. Biophys. Acta, Lipids Lipid Metab., 835: 477-490 (1985).
5. Anthonsen, H., A. Baptista, F. Drablos, P. Martel, S. Petersen, M. Sebastiao, and L. Vaz. Lipases and esterases: A review of their sequences, structure, and evolution, pp. 315-371. In: Biotechnology Annual Review, Vol. 1 (M. El-Gewely, Ed.). Amsterdam: Elsevier (1995).
6. Armand, M. Lipases and lipolysis in the human digestive tract: Where do we stand? Curr. Opin. Clin. Nutr. Metab. Care, 10: 156-164 (2007).
7. Arnault, F., J. Etienne, L. Noe, A. Raisonnier, D. Brault, J. W. Harney, M. J. Berry, C. Tse, C. Fromental-Ramain, J. Hamelin, and F. Galibert. Human lipoprotein lipase last exon is not translated in contrast to lower vertebrates. J. Mol. Evol., 43: 109-115 (1996).
8. Aryee, A. N. A., B. K. Simpson, and R. Villalonga. Lipase fraction from the viscera of grey mullet (Mugil cephalus). Isolation, partial purification, and some biochemical characteristics. Enzyme Microb. Technol, 40: 394-402 (2007).
9. Baba, T., D. Downs, K. W. Jackson, J. Tang, and C.-S. Wang. Structure of human milk bile salt activated lipase. Biochemistry, 30: 500-510 (1991).
10. Berglund, L., J. Khoo, D. Jensen, and D. Steinberg. Resolution of hormone-sensitive triglyceride/diglyceride lipase from monoglyceride lipase of chicken adipose tissue. J. Biol. Chem., 255: 5420-5428 (1980).
11. Bezbradica, D., D. Mijin, S. Siler-Marinkovic, and Z. Knezevic. The effect of substrate polarity on the lipase-catalyzed synthesis of aroma esters in solvent-free systems. J. Mol. Catal B: Enzym., 45: 97-101 (2007).
12. Bier, M. Lipases: RCOOR' + H20 → RCOOH + R'OH, pp. 627-642. In: Methods in Enzymology, Vol. 1 (S. Colowick, and N. Kaplan, Eds.). New York: Academic Press (1955).
13. Biesiot, P. M., and J. M. Capuzzo. Digestive protease, lipase, and amylase activities in stage I larvae of the American lobster, Homarus americanus. Comp. Biochem. Physiol. A: Comp. Physiol., 95:47-54 (1990).
14. Bilinski, E., and Y. C. Lau. Lipolytic activity toward, long-chain triglycerides in lateral line muscle of rainbow trout (Salmo gairdneri). J. Fish Res. Board Can., 26: 1857-1866 (1969).
15. Blackberg, L., and O. Hernell. Bile salt-stimulated lipase in human milk: Evidence that bile salt induces lipid binding and activation via binding to different sites. FEBS Lett., 323: 207-210 (1993).
16. Bolasina, S., A. Perez, and Y. Yamashita. Digestive enzymes activity during ontogenetic development and effect of starvation in Japanese flounder, Paralichthys olivaceus. Aquaculture, 252:503-515(2006).
17. Borgstrom, B., and C. Erlanson. Pancreatic lipase and co-lipase. Interactions and effects of bile salts and other detergents. Eur. J. Biochem., 37: 60-68 (1973).
18. Borlongan, I. G. Studies on the digestive lipases of milkfish, Chanos chonos. Aquaculture, 89: 315-325 (1990).
19. Bornscheuer, U. T. Methods to increase enantioselectivity of lipases and esterases. Curr. Opin. Biotechnol., 13: 543-547 (2002).
20. Bott, R., J. Shield, and A. Poulose. Protein engineering of lipases, pp. 337-354. In: Lipases-Their Structure, Biochemistry, and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
21. Breivik, H., G. G. Haraldsson, and B. Kristinsson. Preparation of highly purified concentrates of eicosapentaenoic acid and docosahexaenoic acid. J. Am. Oil Chem. Soc., 74: 1425-1429 (1997).
22. Brockman, H. L. Triglyceride lipase from porcine pancreas: EC 3.1.1.3. Triacylglycerol acylhydrolase, pp. 619-627. In: Methods in Enzymology, Vol. 71 (J. M. Lowenstein, Ed.). New York: Academic Press (1981).
23. Canioni, P., A. Benajiba, R. Julien, J. Rathelot, A. Benabdeljlil, and L. Sarda. Ovine pancreatic lipase: Purification and some properties. Biochimie, 57: 35-41 (1975).
24. Cao, L. Carrier-bound immobilised enzymes: Principles, applications, and design. Weinheim: Germany: Wiley-VCH (2005).
25. Carriere, F., Y. Gargouri, H. Moreau, S. Ransac, E. Rogalska, and R. Verger. Gastric lipases: Cellular, biochemical, and kinetic aspects, pp. 181-205. In: Lipases-Their Structure, Biochemistry, and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
26. Carriere, F., C. Withers-Martinez, H. van Tilbeurgh, A. Roussel, C. Cambillau, and R. Verger. Structural basis for the substrate selectivity of pancreatic lipases and some related proteins. Biochim. Biophys. Acta, Rev. Biomembr., 1376: 417-432 (1998).
27. Castro, G. R., and T. Knubovets. Homogenous biocatalysis in organic solvents and water-organic mixtures. Crit. Rev. Biotechnol., 23: 195-231 (2003).
28. Chesley, L. C. The concentrations of proteases, amylase, and lipase in certain marine fishes. Biol. Bull., 66: 133-144 (1934).
29. Choi, S. Y., K.-I. Hirata, T. Ishida, T. Quertermous, and A. D. Cooper. Endothelial lipase: A new lipase on the block. J. Lipid Res., 43: 1763-1769 (2002).
30. Christensen, M., L. Andersen, T. Husum, and O. Kirk. Industrial lipase immobilization. Eur. J. Lipid Sci. Technol., 105: 318-321 (2003).
31. Connelly, P. W. The role of hepatic lipase in lipoprotein metabolism. Clin. Chim. Acta, 286: 243-255 (1999).
32. Crenon, I., E. Foglizzo, B. Kerfelec, A. Verine, D. Pignol, J. Hermoso, J. Bonicel, and C. Chapus. Pancreatic lipase-related protein type I: A specialized lipase or an inactive enzyme. Protein Eng., 11: 135-142 (1998).
33. Das, K. M., and S. D. Tripathi. Studies on the digestive enzymes of grass carp, Ctenopharyngodon idella (Val.). Aquaculture, 92: 21-32 (1991).
34. De Caro, J., M. Boudouard, J. Bonicel, A. Guidoni, P. Desnuelle, and M. Rovery. Porcine pancreatic lipase. Completion of the primary structure. Biochim. Biophys. Acta, Protein Struct., 671: 129-138 (1981).
35. Diaz-Lopez, M., and F. Garcia-Carreno. Applications of fish and shellfish enzymes in food and feed products, pp. 571-618. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality (N. F. Haard and B. K. Simpson, Eds.). New York: Marcel Dekker (2000).
36. Egmond, M. Application of lipolytic enzymes in detergents, pp. 655-661. In: Lipid Biotechnology (T. Kuo and H. Gardner, Eds.). New York: Marcel Dekker (2002).
37. Erlanson, C. Purification, properties, and substrate specificity of a carboxylesterase in pancreatic juice. Scand. J. Gastroent., 10: 401-408 (1975).
38. Erlanson, C., P. Fernlund, and B. Borgstrom. Purification and characterization of two proteins with co-lipase activity from porcine pancreas. Biochim. Biophys. Acta, Protein Struct., 310: 437-445 (1973).
39. FAO. The State of World Fisheries and Aquaculture 2006. Rome: FAO Fisheries and Aquaculture Department (2007).
40. Ferrato, F., F. Carriere, L. Sarda, and R. Verger. A critical reevaluation of the phenomenon of interfacial activation, pp. 327-347. In: Methods in Enzymology, Vol. 286 (B. Rubin and E. A. Dennis, Eds.). New York: Academic Press (1997).
41. Gargouri, Y., R. Julien, G. Pieroni, R. Verger, and L. Sarda. Studies on the inhibition of pancreatic and microbial lipases by soybean proteins. J. Lipid Res., 25: 1214-1221 (1984).
42. Gargouri, Y., S. Ransac, and R. Verger. Covalent inhibition of digestive lipases: An in vitro study. Biochim. Biophys. Acta, Lipids Lipid Metab., 1344: 6-37 (1997).
43. Georlette, D., V. Blaise, T. Collins, S. D'Amico, E. Gratia, A. Hoyoux, J.-C. Marx, G. Sonan, G. Feller, and C. Gerday. Some like it cold: Biocatalysis at low temperatures. FEMS Microbiol. Rev., 28: 25-42 (2004).
44. Gidez, L. I. Purification of rat pancreatic lipase. J. Lipid Res., 9: 794-798 (1968).
45. Gildberg, A., B. K. Simpson, and N. F. Haard. Uses of enzymes from marine organisms, pp. 619-639. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality (N. F. Haard and B. K. Simpson, Eds.). New York: Marcel Dekker (2000).
46. Gilham, D., and R. Lehner. Techniques to measure lipase and esterase activity in vitro. Methods, 36: 139-147 (2005).
47. Gjellesvik, D. R. Fatty acid specificity of bile salt-dependent lipase: Enzyme recognition and super-substrate effects. Biochim. Biophys. Acta, Lipids Lipid Metab., 1086: 167-172 (1991).
48. Gjellesvik, D. R., D. Lombardo, and B. T. Walther. Pancreatic bile salt dependent lipase from cod (Gadus morhua): Purification and properties. Biochim. Biophys. Acta, Lipids Lipid Metab., 1124: 123-134 (1992).
49. Gjellesvik, D. R., J. B. Lorens, and R. Male. Pancreatic carboxylester lipase from Atlantic salmon (Salmo salar). cDNA sequence and computer-assisted modelling of tertiary structure. Eur. J. Biochem., 226: 603-612 (1994).
50. Gjellesvik, D. R., A. J. Raae, and B. T. Walther. Partial purification and characterization of a triglyceride lipase from cod (Gadus morhua). Aquaculture, 79: 177-184 (1989).
51. Goldberg, I. Lipoprotein lipase and lipolysis: Central roles in lipoprotein metabolism and atherogenesis. J. Lipid Res., 37: 693-707 (1996).
52. Gupta, M. N. Enzyme function in organic solvents. Eur. J. Biochem., 203: 25-32 (1992).
53. Gupta, R., P. Rathi, and S. Bradoo. Lipase mediated upgradation of dietary fats and oils. Crit. Rev. Food Sci. Nutr., 43: 635-644 (2003a).
54. Gupta, R., P. Rathi, N. Gupta, and S. Bradoo. Lipase assays for conventional and molecular screening: An overview. Biotechnol, Appl Biochem., 37: 63-71 (2003b).
55. Guy, R. C. E., and S. S. Sahi. Application of a lipase in cake manufacture. J. Sci. Food Agric., 86: 1679-1687 (2006).
56. Haas, M., G. Piazza, and T. Foglia. Enzymatic approaches to the production of biodiesel fuels, pp. 587-598. In: Lipid Biotechnology (T. Kuo and H. Gardner, Eds.). New York: Marcel Dekker (2002).
57. Halford, J. C. G. Pharmacotherapy for obesity. Appetite, 46: 6-10 (2006).
58. Halldorsson, A., C. D. Magnusson, and G. G. Haraldsson. Chemoenzymatic synthesis of structured triacylglycerols. Tetrahedron Lett., 42: 7675-7677 (2001).
59. Hama, S., H. Yamaji, T. Fukumizu, T. Numata, S. Tamalampudi, A. Kondo, H. Noda, and H. Fukuda. Biodiesel-fuel production in a packed-bed reactor using lipase-producing Rhizopus oryzae cells immobilized within biomass support particles. Biochem. Eng. J., 34: 273-278 (2007).
60. Han, J. H., C. Stratowa, and W. J. Rutter. Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning. Biochemistry, 26: 1617-1625 (1987).
61. Haraldsson, G. G., A. Halldorsson, and E. Kulås. Chemoenzymatic synthesis of structured triacylglycerols containing eicosapentaenoic and docosahexaenoic acids. J. Am. Oil Chem. Soc., 77: 1139-1145 (2000).
62. Hargrove, J. L., P. Greenspan, and D. K. Hartle. Nutritional significance and metabolism of very long chain fatty alcohols and acids from dietary waxes. Exp. Biol. Med., 229: 215-226 (2004).
63. Harmon, J., K. Michelsen, and M. A. Sheridan. Purification and characterization of hepatic triacylglycerol lipase isolated from rainbow trout, Oncorhynchus mykiss. Fish Physiol. Biochem., 9: 361-368 (1991).
64. Harmon, J. S., L. M. Rieniets, and M. A. Sheridan. Glucagon and insulin regulate lipolysis in trout liver by altering phosphorylation of triacylglycerol lipase. Am. J. Physiol., Regul Integr. Comp. Physiol., 265: 255-260 (1993).
65. Hazarika, S., P. Goswami, N. N. Dutta, and A. K. Hazarika. Ethyl oleate synthesis by porcine pancreatic lipase in organic solvents. Chem. Eng. J., 85: 61-68 (2002).
66. Hermoso, J., D. Pignol, B. Kerfelec, I. Crenon, C. Chapus, and J. C Fontecilla-Camps. Lipase activation by nonionic detergents, the crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J. Biol. Chem., 271:18007-18016 (1996).
67. Hide, W., L. Chan, and W. Li. Structure and evolution of the lipase superfamily. J. Lipid Res., 33: 167-178 (1992).
68. Hiol, A., M. D. Jonzo, N. Rugani, D. Druet, L. Sarda, and. L. C. Comeau. Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit. EnzymeMicrob. Technol., 26: 421-430 (2000).
69. Hoehne-Reitan, K., E. Kjorsvik, and D. R. Gjellesvik. Development of bile salt-dependent lipase in larval turbot. J. Fish Biol., 58: 737-745 (2001a).
70. Hoehne-Reitan, K., E. Kjorsvik, and K. I. Reitan. Bile salt-dependent lipase in larval turbot, as influenced by density and lipid content of fed prey. J. Fish Biol., 58: 746-754 (2001b).
71. Hoehne-Reitan, K., E. Kjorsvik, and K. I. Reitan. Lipolytic activities in developing turbot larvae as influenced by diet. Aquaculture Int., 11: 477-489 (2003).
72. Hou, C. Industrial uses of lipases, pp. 387-397. In: Lipid Biotechnology (T. Kuo and H. Gardner, Eds.). New York: Marcel Dekker (2002).
73. Hui, D. Y., and P. N. Howles. Carboxyl ester lipase: Structure-function relationship and physiological role in lipoprotein metabolism and atherosclerosis. J. Lipid Res., 43: 2017-2030 (2002).
74. Huit, K., and P. Berglund. Engineered enzymes for improved organic synthesis. Curr. Opin. Biotechnol., 14: 395-400 (2003).
75. Hyun, J., H. Kothari, E. Herm, J. Mortenson, C. R. Treadwell, and G. V. Vahouny. Purification and properties of pancreatic juice cholesterol esterase. J. Biol. Chem., 244: 1937-1945 (1969).
76. Iijima, N., S. Tanaka, and Y. Ota. Purification and characterization of bile salt-activated lipase from the hepatopancreas of red sea bream, Pagrus major. Fish Physiol. Biochem., 18: 59-69 (1998).
77. Iizuka, K., H. Higurashi, J. Fujimoto, Y. Hayashi, K. Yamamoto, and H. Hiura. Purification of human pancreatic lipase and the influence of bicarbonate on lipase activity. Ann. Clin. Biochem., 28: 373-378 (1991).
78. Itabashi, Y., and T. Ota. Lipase activity in scallop hepatopancreas. Fish. Sci., 60: 347 (1994).
79. Izquierdo, M. S., and R. J. Henderson. The determination of lipase and phospholipase activities in gut contents of turbot (Scophthalmus maximus) by fluorescence-based assays. Fish Physiol. Biochem., 19: 153-162 (1998).
80. Jansen, H., A. J. M. Verhoeven, and E. J. G. Sijbrands. Hepatic lipase: A pro- or anti-atherogenic protein? J. Lipid Res., 43: 1352-1362 (2002).
81. Ju, S.-J., and H. R. Harvey. Lipids as markers of nutritional condition and diet in the Antarctic krill Euphausia superba and Euphausia crystallorophias during austral winter. Deep-sea Res. II, 51: 2199-2214 (2004).
82. Julien, R., P. Canioni, J. Rathelot, L. Sarda, and T. H. Plummer Jr. Studies on bovine pancreatic lipase and colipase. Biochim. Biophys. Acta, Lipids Lipid Metab., 280: 215-224 (1972).
83. Kaneniwa, M., M. Yokoyama, Y. Murata, and R. Kuwahara. Enzymatic hydrolysis of lipids in muscle of fish and shellfish during cold storage. Adv. Exp. Med. Biol., 542: 113-119 (2004).
84. Klibanov, A. M. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci., 14: 141-144 (1989).
85. Koo, S. I., and S. K. Noh. Green tea as inhibitor of the intestinal absorption of lipids: Potential mechanism for its lipid-lowering effect. J. Nutr. Biochem., 18: 179-183 (2007).
86. Kojima, Y., E. Sakuradani, and S. Shimizu. Different specificity of two types of Pseudomonas lipases for C20 fatty acids with a Δ5 unsaturated double bond and their application for selective concentration of fatty acids. J. Biosci. Bioeng., 101: 496-500 (2006).
87. Kojima, Y., and. S. Shimizu. Purification and characterization of the lipase from Pseudomonas fluorescens HU380. J. Biosci. Bioeng., 96: 219-226 (2003).
88. Kotting, J., and H. Eibl. Lipases and phospholipases in organic synthesis, pp. 289-314. In: Lipases-Their Structure, Biochemistry, and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
89. Koven, W. M., R. J. Henderson, and J. R. Sargent. Lipid digestion in turbot (Scophthalmus maximus). 1. Lipid class and fatty acid composition of digesta from different segments of the digestive tract. Fish Physiol. Biochem., 13: 69-79 (1994a).
90. 14-labeled triacylglycerol, cholesterol ester, and phosphatidylcholine by digesta from different segments of the digestive tract. Fish Physiol. Biochem., 13: 275-283 (1994b).
91. Koven, W. M., R. J. Henderson, and J. R. Sargent. Lipid digestion in turbot (Scophthalmus maximus): In vivo and in vitro studies of the lipolytic activity in various segments of the digestive tract. Aquaculture, 151: 155-171 (1997).
92. Kraemer, F. B., and W.-J. Shen. Hormone-sensitive lipase: Control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis. J. Lipid Res. 43: 1585-1594 (2002).
93. Kwon, D., and J. Rhee. A simple and rapid colorimetric method for determination of free fatty acids for lipase activity. J. Am. Oil Chem. Soc., 63: 89-92 (1986).
94. Kyger, E. M., R. C. Wiegand, and L. G. Lange. Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase. Biochem. Biophys. Res. Commun., 164: 1302-1309 (1989).
95. Lai, D. T., and. C. J. O'Connor. Studies on synthesis of short chain alkyl esters catalyzed by goat pregastric lipase. J. Mol. Catal. B: Enzym., 6: 411-420 (1999).
96. Lai, D. T., R. D. Stanley, and C. J. O'Connor. Purification of pregastric lipases of caprine origin. J. Am. Oil Chem. Soc., 75:411-416 (1998).
97. Lee, R. F., J. C. Nevenzel, and G. A. Paffenhofer. Wax esters in marine copepods. Science, 167: 1510-1511 (1970).
98. Leger, C. Essai de purification de la lipase de tissu intercaecal de la truite (Salmo gairdneri Rich.). Ann. Biol. Anim. Biochem. Biophys., 12: 341-345 (1972).
99. Leger, C., and D. Bauchart. Hydrolyse de triglycerides par le systeme lipasique du pancreas de truite. Mise en evidence d'un nouveau type de specificite d'action. C. R. Hebd. Seanc Acad. Sci., Paris, 275: 2419-2422 (1972).
100. 2+, gel filtrations. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 57: 359-363 (1977).
101. Leger, C., P. Bergot, J. Flanzy, and A. Francois. Mise en evidence d'une activite lipasique dans le pancreas diffuse de la truite. Etude de modalites d'action de l'enzyme responsible. C. R. Hebd Seanc. Acad. Sci., Paris, 270: 2813-2816 (1970).
102. Leger, C., V Ducruet, and J. Flanzy. Lipase et colipase de la truite arc-en-ciel. Quelques resultats recents. Ann. Biol. Anim. Biochim. Biophys., 19: 825-832 (1979).
103. Lie, O., and G. Lambertsen. Digestive lipolytic enzymes in cod (Gadus morhua): Fatty acid specificity. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 80: 447-450 (1985).
104. Lie, O., and G. Lambertsen. Lipid digestion and absorption in cod (Gadus morhua), comparing triacylglycerols, wax esters and diacylalkylglycerols. Comp. Biochem. Physiol., A: Comp. Physiol., 98: 159-163 (1991).
105. Lie, O., E. Lied, and G. Lambertsen. Lipid digestion in cod (Gadus morhua). Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 88: 697-700 (1987).
106. Lima, V.M. G., N. Krieger, D. A. Mitchell, and J. D. Fontana. Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents. Biochem. Eng. J., 18: 65-71 (2004).
107. Lindberg, A., and G. Olivecrona. Lipase evolution - trout, Xenopus and chicken have lipoprotein-lipase and apolipoprotein C-II-like activity but lack hepatic lipase-like activity. Biochim. Biophys. Acta, Lipids Lipid Metab., 1255: 205-211 (1995).
108. Lombardo, D., O. Guy, and C. Figarella. Purification and characterization of a carboxyl ester hydrolase from human pancreatic juice. Biochim. Biophys. Acta, Enzymol., 527: 142-149 (1978).
109. Lopez-Amaya, C., and A. G. Marangoni. Lipases, pp. 121-146. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality (N. F. Haard and B. K. Simpson, Eds.). New York: Marcel Dekker (2000a).
110. Lopez-Amaya, C., and A. G. Marangoni. Phospholipases, pp. 91-119. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality (N. F. Haard and B. K. Simpson, Eds.). New York: Marcel Dekker (2000b).
111. Lowe, M. E. The triglyceride lipases of the pancreas. J. Lipid Res., 43: 2007-2016 (2002).
112. Lutz, S. Engineering lipase B from Candida antarctica. Tetrahedron: Asym., 15: 2743-2748 (2004).
113. Marchetti, J. M., V. U. Miguel, and A. F. Errazu. Possible methods for biodiesel production. Renew. Sustain. Energy Rev., 11: 1300-1311 (2007).
114. Martinelle, M., and K. Hult. Kinetics of triglyceride lipases, pp. 159-180. In: Lipases - Their Structure, Biochemistry, and Application (P. Wooley and S.B. Petersen, Eds.). Cambridge:Cambridge University Press (1994).
115. Mateo, C., J. M. Palomo, G. Fernandez-Lorente, J. M. Guisan, and R. Fernandez-Lafuente. Improvement of enzyme activity, stability, and selectivity via immobilization techniques. Enzyme Microb. Technol., 40: 1451-1463 (2007).
116. Matori, M., T. Asahara, and Y. Ota. Positional specificity of microbial lipases. J. Ferment. Bioeng., 72: 397-398 (1991).
117. Maurin, C., and Y. Gal. Characterization of a hydrophobic esterase from tuna (Thunnus albacares) pyloric caeca. J. Mar. Biotechnol., 4: 87-90 (1996).
118. McGinnis, L., and M. Wood. Finding new uses for fish byproducts. Agric. Res., 55: 18-19 (2007).
119. Mejdoub, H., J. Reinbolt, and Y. Gargouri. Dromedary pancreatic lipase: Purification and structural properties. Biochim. Biophys. Acta, Lipids Lipid Metab., 1213: 119-126 (1994).
120. Merkel, M., R. H. Eckel, and I. J. Goldberg. Lipoprotein lipase: Genetics, lipid uptake, and regulation. J. Lipid Res., 43: 1997-2006 (2002).
121. Michelsen, K. G., J. S. Harmon, and M. A. Sheridan. Adipose tissue lipolysis in rainbow trout, Oncorhynchus mykiss, is modulated by phosphorylation of triacylglycerol lipase. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 107: 509-513 (1994).
122. Miled, N., M. Riviere, J. F. Cavalier, G. Buono, L. Berti, and R. Verger. Discrimination between closed and open forms of lipases using electrophoretic techniques. Anal. Biochem., 338: 171-178 (2005).
123. Momsen,W. E., and H. L. Brockman. Purification and characterization of cholesterol esterase from porcine pancreas. Biochim. Biophys. Acta, Lipids Lipid Metab., 486: 103-113 (1977).
124. Moore, S. A., R. L. Kingston, K. M. Loomes, O. Hernell, L. Blackberg, H. M. Baker, and E.N. sBaker. The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding. J. Mol. Biol., 312: 511-523 (2001).
125. Mukherjee, K. Plant lipases as biocatalysts, pp. 399-415. In: Lipid Biotechnology (T. Kuo and H. Gardner, Eds.). New York: Marcel Dekker (2002).
126. Mukherjee, K., and M. Hills. Lipases from plants, pp. 49-75. In: Lipases - Their Structure, Biochemistry, and Application (P.Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
127. Mukherjee, M. Human digestive andmetabolic lipases - a brief review. J. Mol. Catal. B: Enzym., 22: 369-376 (2003).
128. Mukundan, M. K., K. Gopakumar, and M. R. Nair. Purification of a lipase from the hepatopancreas of oil sardine (Sardinella longiceps Linnaeus) and its characteristics and properties. J. Sci. Food Agric., 36: 191-203 (1985).
129. Nayak, J., P.G.V. Nair, K. Ammu, and S. Mathew. Lipase activity in different tissues of four species of fish: Rohu (Labeo rohita Hamilton), oil sardine (Sardinella Iongiceps Linnaeus), mullet (Liza subviridis Valenciennes) and Indian mackerel (Rastrelliger kanagurta Cuvier). J. Sci. Food Agric., 83: 1139-1142 (2003).
130. Nie, K., F. Xie, F. Wang, and T. Tan. Lipase catalyzed methanolysis to produce biodiesel: Optimization of the biodiesel production. J. Mol. Catal. B: Enzym., 43: 142-147 (2006).
131. Nini, L., L. Sarda, L.-C. Comeau, E. Boitard, J.-P. Dubes, and H. Chahinian. Lipase-catalysed hydrolysis of short-chain substrates in solution and in emulsion: A kinetic study. Biochim. Biophys. Acta, Mol. Cell Biol. Lipids, 1534: 34-44 (2001).
132. O'Connor, C. J., and R. D. Manuel. Inhibiting the activity of calf pregastric lipase: Effect of bile salts, lecithin, liposomes, phenyl boronic acid, and diethyl 4-nitrophenyl phosphate. J. Bioact. Compat. Polym., 15: 489-502 (2000).
133. Oku, H., N. Koizumi, T. Okumura, T. Kobayashi, and T. Umino. Molecular characterization of lipoprotein lipase, hepatic lipase, and pancreatic lipase genes: Effects of fasting and refeeding on their gene expression in red sea bream Pagrus major. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 145: 168-178 (2006).
134. Olempska-Beer, Z. S., R. I. Merker, M. D. Ditto, and M. J. DiNovi. Food-processing enzymes from recombinant microorganisms - a review. Regul. Toxicol. Pharm., 45: 144-158 (2006).
135. Olsen, R. E., R. J. Henderson, and E. Ringo. The digestion and selective absorption of dietary fatty acids in Arctic charr, Salvelinus alpinus. Aquac. Nutr., 4: 13-21 (1998).
136. Overnell, J. Digestive enzymes of the pyloric caeca and of their associated mesentery in the cod (Gadus morhua). Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 46: 519-531 (1973).
137. Palekar, A. A., P. T. Vasudevan, and S. Yan. Purification of lipase: A review. Biocatal. Biotransform., 18: 177-200 (2000).
138. Pandey, A., C. R. Soccol, N. Krieger, S. Benjamin, P. Nigam, and V. T. Soccol. The realm ofmicrobial lipases in biotechnology. Biotechnol. Appl. Biochem., 29: 119-131 (1999).
139. Patel, R. Enzymatic preparation of chiral pharmaceutical intermediates by lipases, pp. 527-561. In: Lipid Biotechnology (T. Kuo and H. Gardner, Eds.). New York: Marcel Dekker (2002).
140. Patkar, S., and F. Bjorkling. Lipase inhibitors, pp. 207-224. In: Lipases - Their Structure, Biochemistry, and Application (P.Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
141. Patton, J. S. High levels of pancreatic nonspecific lipase in rattlesnake and leopard shark. Lipids, 10: 562-564 (1975).
142. Patton, J. S., J. C. Nevenzel, and A. A. Benson. Specificity of digestive lipases in hydrolysis of wax esters and triglycerides studied in anchovy and other selected fish. Lipids, 10: 575-583 (1975).
143. Patton, J. S., and J. G. Quinn. Studies on the digestive lipase of the surf clam (Spisula solidissima). Mar. Biol., 21: 59-69 (1973).
144. Patton, J. S., T. G. Warner, and A. A. Benson. Partial characterization of the bile salt dependent triacylglycerol lipase from the leopard shark pancreas. Biochim. Biophys. Acta,Lipids Lipid Metab., 486: 322-330 (1977).
145. Pencreac'h, G., and J. C. Baratti. Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: A simple test for the determination of lipase activity in organic media. Enzyme Microb. Technol., 18: 417-422 (1996).
146. Perret, B., L. Mabile, L. Martinez, F. Terce, R. Barbaras, and X. Collet. Hepatic lipase: Structure/function relationship, synthesis, and regulation. J. Lipid Res., 43: 1163-1169 (2002).
147. Petersen, M. T. N., P. Fojan, and S. B. Petersen. How do lipases and esterases work: The electrostatic contribution. J. Biotechnol., 85: 115-147 (2001).
148. Pignol, D., J. Hermoso, B. Kerfelec, I. Crenon, C. Chapus, and J. Carlos Fontecilla-Camps. The lipase/colipase complex is activated by a micelle: Neutron crystallographic evidence. Chem. Phys. Lipids, 93: 123-129 (1998).
149. Ramarethinam, S., K. Latha, andN. Rajalakshmi. Use of a fungal lipase for enhancement of aroma in black tea. Food Sci. Technol. Res., 8: 328-332 (2002).
150. Rasco, B. A., and H. O. Hultin. A comparison of dogfish and porcine pancreatic lipases. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 89: 671-677 (1988).
151. Reue, K., J. Zambaux, H.Wong, G. Lee, T. Leete, M. Ronk, J. Shively, B. Sternby, B. Borgstrom, and D. Ameis. cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit. J. Lipid Res., 32: 267-276 (1991).
152. Robles Medina, A., L. Esteban Cerdan, A. Gimenez Gimenez, B. Camacho Paez, M. J. Ibanez Gonzalez, and E. Molina Grima. Lipasecatalyzed esterification of glycerol and polyunsaturated fatty acids from fish and microalgae oils. J. Biotechnol., 70: 379-391 (1999).
153. Rocha-Uribe, A., and E. Hernandez. Solvent-free enzymatic synthesis of structured lipids containing CLA from coconut oil and tricaprylin. J. Am. Oil Chem. Soc., 81: 685-689 (2004).
154. Rudd, E. A., N. K.Mizuno, and H. L. Brockman. Isolation of two forms of carboxylester lipase (cholesterol esterase) from porcine pancreas. Biochim. Biophys. Acta, Lipids Lipid Metab., 918: 106-114 (1987).
155. Saito H., Y. Kotani, J. M. Keriko, C. Xue, K. Taki, K. Ishihara, T. Ueda, and S. Miyata. High levels of n-3 polyunsaturated fatty acids in Euphausia pacifica and its role as a source of docosahexaenoic and icosapentaenoic acids for higher trophic levels. Mar. Chem., 78: 9-28 (2002).
156. Salleh, A. B., M. Basri, M. Taib, H. Jasmani, R. N. Z. A. Rahman, M. B. A. Rahman, and C. N. A. Razak. Modified enzymes for reactions in organic solvents. Appl. Biochem. Biotechnol., 102-103: 349-357 (2002).
157. Sarda, L., G. Marchis-Mouren, and P. Desnuelle. Nouveaux essais de purification de la lipase pancreatique de porc. Biochimica et Biophysica Acta, 30: 224 (1958).
158. Satouchi, K., K. Hirano, O. Fujino, M. Ikoma, T. Tanaka, and K. Kitamura. Lipoxygenase-1 from soybean seed inhibiting the activity of pancreatic lipase. Biosci. Biotechnol. Biochem., 62: 1498-1503 (1998).
159. Satouchi, K., Y. Kodama, K. Murakami, T. Tanaka,H. Iwamoto, and M. Ishimoto. A lipase-inhibiting protein from lipoxygenase-deficient soybean seeds. Biosci. Biotechnol. Biochem., 66: 2154-2160 (2002).
160. Sayari, A., H. Mejdoub, and Y. Gargouri. Characterization of turkey pancreatic lipase. Biochimie, 82: 153-159 (2000).
161. Schmidt, M., and U. T. Bornscheuer. High-throughput assays for lipases and esterases. Biomol. Eng., 22: 51-56 (2005).
162. Schrag, J. D., and M. Cygler. Lipases and α/β hydrolase fold, pp. 85-107. In: Methods in Enzymology, Vol. 284 (B. Rubin and E. A. Dennis, Eds.). New York: Academic Press (1997).
163. Shah, S., and M. N. Gupta. Lipase catalyzed preparation of biodiesel from Jatropha oil in a solvent free system. Process Biochem., 42: 409-414 (2007).
164. Shahani, K. M., I. M. Khan, and R. C. Chandan. Bovine pancreatic lipase. I. Isolation, homogeneity, and characterization. J. Dairy Sci., 59: 369-375 (1976).
165. Sharma, R., Y. Chisti, and U. C. Banerjee. Production, purification, characterization, and applications of lipases. Biotechnol. Adv., 19: 627-662 (2001).
166. Sharma, N., V. K. Sharma, and S.-Y. Seo. Screening of some medicinal plants for anti-lipase activity. J. Ethnopharmacol., 97: 453-456 (2005).
167. Sheridan,M.A., andW.V.Allen. Partial purification of a triacylglycerol lipase isolated from steelhead trout (Salmo gairdneri) adipose tissue. Lipids, 19: 347-352 (1984).
168. Simpson, B. K. Digestive proteinases from marine animals. pp. 191-213. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality (N. F. Haard and B. K. Simpson, Eds.). New York: Marcel Dekker (2000).
169. Steiner, J. M., and D. A. Williams. Purification of classical pancreatic lipase from dog pancreas. Biochimie, 84: 1243-1251 (2002).
170. Steiner, J. M., B. G. Wilson, and D. A. Williams. Purification and partial characterization of feline classical pancreatic lipase. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 134: 151-159 (2003).
171. Sidell, B. D., and J. R. Hazel. Triacylglycerol lipase activities in tissues of Antarctic fishes. Polar Biol., 25: 517-522 (2002).
172. Sternby, B., A. Engstrom, and U. Hellman. Purification and characterization of pancreatic colipase from the dogfish (Squalus acanthius). Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 789: 159-163 (1984).
173. Sternby, B., A. Larsson, and B. Borgström. Evolutionary studies on pancreatic colipase. Biochim. Biophys. Acta, Lipids Lipid Metab., 750: 340-345 (1983).
174. Sukarno, K. Takahashi, M. Hatano, and Y. Sakurai. Lipase from neon flying squid hepatopancreas: Purification and properties. Food Chem., 57: 515-521 (1996).
175. Svendsen, A. Sequence comparisons within the lipase family, pp. 1-21. In: Lipases - Their Structure, Biochemistry, and Application (P. Wooley and S.B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
176. Svendsen, A. Lipase protein engineering. Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 1543: 223-238 (2000).
177. Taipa, M. A., M. R. Aires-Barros, and J. M. S. Cabral. Purification of lipases. J. Biotechnol., 26: 111-142 (1992).
178. Taniguchi, A., K. Takano, and I. Kamoi. Purification and properties of lipase from Tilapia intestine - digestive enzyme of Tilapia - VI. Nippon Suisan Gakk., 67: 78-84 (2001).
179. Teo, L. H., and U. Sabapathy. Preliminary report on the digestive enzymes present in the digestive gland of Perna viridis. Mar. Biol., 106: 403-407 (1990).
180. Tocher, D. R., and J. R. Sargent. Studies on triacylglycerol, wax ester, and sterol ester hydrolases in intestinal caeca of rainbowtrout (Salmo gairdneri) fed diets rich in triacylglycerols and wax esters. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 77: 561-571 (1984).
181. Torres, S., and G. R. Castro. Non-aqueous biocatalysis in homogenous solvent systems. Food Technol. Biotechnol., 42: 271-277 (2004).
182. Torres, C. F., H. S. Garcia, J. J. Ries, and C. G. Hill. Esterification of glycerol with conjugated linoleic acid and long-chain fatty acids from fish oil. J. Am. Oil Chem. Soc., 78: 1093-1098 (2001).
183. Tsujita, T., Y. Matsuura, and H. Okuda. Studies on the inhibition of pancreatic and carboxylester lipases by protamine. J. Lipid Res., 37: 1481-1487 (1996).
184. Vandermeers, A., M. C.Vandermeers-Piret, J. Rathe, and J. Christophe. On human pancreatic triacylglycerol lipase: Isolation and some properties. Biochim. Biophys. Acta, Enzymol., 370: 257-268 (1974).
185. van den Bosch, H., A. J. Aarsman, J. G. N. De Jong, and L. L. M. Van Deenen. Studies on lysophospholipases: I. Purification and some properties of a lysophospholipase from beef pancreas. Biochim. Biophys. Acta, Lipids Lipid Metab., 296: 94-104 (1973).
186. van Tilbeurgh, H., S. Bezzine, C. Cambillau, R. Verger, and F. Carriere. Colipase: Structure and interaction with pancreatic lipase. Biochim. Biophys. Acta, Mol. Cell Biol. Lipids, 1441: 173-184 (1999).
187. van Tilbeurgh, H.,M.-P. Egloff, C.Martinez, N. Rugani, R. Verger, and C. Cambillau. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature, 362: 814-820 (1993).
188. Verger, R., G. H. De Haas, L. Sarda, and P. Desnuelle. Purification from porcine pancreas of two molecular species with lipase activity. Biochim. Biophys. Acta, Protein Struct., 188: 272-282 (1969).
189. von Tigerstrom., R. G., and S. Stelmaschuk. The use of Tween 20 in a sensitive turbidimetric assay of lipolytic enzymes. Can. J. Microbiol., 35: 511-514 (1989).
190. Vulfson, E. Industrial applications of lipases, pp. 271-288. In: Lipases-Their Structure, Biochemistry, and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (.1994).
191. Wang, C.-S., and J. A. Hartsuck. Bile salt-activated lipase. A multiple function lipolytic enzyme. Biochim. Biophys. Acta, Lipids Lipid Metab., 1166: 1-19 (1993).
192. Wang, C. S. Purification of human milk bile salt-activated lipase by cholic acid-coupled Sepharose 4B affinity chromatography. Anal. Biochem., 105: 398-402 (1980).
193. Wang, C. S., and K. Johnson. Purification of human milk bile salt-activated lipase. Anal. Biochem., 133: 457-461 (1983).
194. Wang, X., C.-S. Wang, J. Tang, F. Dyda, and X. C. Zhang. The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. Structure, 5: 1209-1218 (1997).
195. Wescott, C. R., and Klibanov, A. M. The solvent dependence of enzyme specificity. Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 1206: 1-9 (1994).
196. Widmer, F. Pancreatic lipase effectors extracted from soybean meal. J. Agric Food Chem., 25: 1142-1145 (1977).
197. Winkler, F. K., A. D'Arcy, and W. Hunziker. Structure of human pancreatic lipase. Nature, 343: 771-774 (1990).
198. Winkler, F. K., and K. Gubernator. Structure and mechanism of human pancreatic lipase, pp. 139-157. In: Lipases-Their Structure, Biochemistry, and Application (P. Wooley and S. B. Petersen, Eds.). Cambridge: Cambridge University Press (1994).
199. Wong, H., and M. C. Schotz. The lipase gene family. J. Lipid Res., 43: 993-999 (2002).
200. Young, D., D. King, M. Chen, B. Norris, and P. Nemeth. A novel method for measurement of triglyceride lipase activity: Suitable for microgram and nanogram quantities of tissue. J. Lipid Res., 29: 527-532 (1988)
201. Zaks, A., and A. M. Klibanov. Enzymatic catalysis in nonaqueous solvents. J. Biol. Chem., 263: 3194-3201 (1988).