Summary
A novel enzyme hydrolysing mono- and diacylglycerol was found in the culture filtrate of an isolated fungus, Penicillium camembertii. The enzyme was separated into two forms (A- and B-enzyme) with almost the same molecular weight (37,000–39,000), amino acid composition and identical N-terminal amino acid sequence. B-Enzyme, a major component, was purified approximately 210-fold with an activity yield of 2.6%. The B-enzyme was specific to mono- and diacylglycerols and hydrolysed long-chain monoacylglycerols most efficiently. Triacylglycerols were completely inert as substrates for the enzyme. The B-enzyme preferred to attack α-position to β-position of monoacylglycerol, but showed no stereospecificity on mono- and diacylglycerol. Both Fe3+ and Hg2+ inhibited B-enzyme activity significantly.
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References
Akesson B, Gronowitz S, Herslof B, Michelsen P, Olivecrona T (1983) Stereospecificity of different lipases. Lipids 18:313–318.
Azuma T (1977) JIS Z 8721 junkyo Hyojun Shikiryo, Nihon Kikaku Kyokai, Tokyo.
Brady L, Brazozowski AM, Derewenda ZS, Dodson G, Tolley S, Turkenberg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343:767–770.
Chopineau J, McCafferty FD, Therisod M, Klibanov AM (1988) Production of biosurfactants from sugar alcohols and vegetable oils catalyzed by lipase in a nonaqueous medium. Biotechnol Bioeng 31:208–214.
Hoq MM, Yamane T, Shimizu S, Funada T, Ishida S (1985) Continuous hydrolysis of olive oil by lipase in microporous hydrophobic membrane bioreactor. J Am Oil Chem Soc 62:1016–1021.
Huge-Jensen B, Galluzzo DR, Jensen RG (1987) Partial purification and characterization of free and immobilized lipases from Mucor miehei. Lipids 22:559–565.
Ikeda Y, Okumura K, Fujii S (1977) Purification and characterization of rat liver microsomal monoacylglycerol lipase in comparison to the other esterases. Biochim Biophys Acta 488:128–139.
Iwai M, Tsujisaka Y (1984) Fungal lipase. In: Borgström B, Brockman HL (eds) Lipases. Elsevier Science Publishers, Amsterdam, pp 443–469.
Kirchner G, Scollar MP, Klivanov AM (1985) Resolution of racemic mixtures via lipase catalysis in organic solvents. J Am Chem Soc 107:7072–7076.
Linfield WM, O'Brien DJ, Serata S, Barauskas RA (1984) Lipid-lipase interactions. I. Fat splitting with lipase from Candida rugosa. J Am Oil Chem Soc 61:1067–1071.
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275.
Nagao A, Kito M (1989) Synthesis of O-acyl-l-homoserine by lipase. J Am Oil Chem Soc 66:710–713.
Okumura S, Iwai M, Tsujisaka Y (1980) Purification and properties of partial glyceride hydrolase of Penicillium cyclopium M1. J Biochem 87:205–211.
Pitt JI (1979) Chapter 4. Isolation, cultivation and preservation, p. 16. Chapter 10. Subgenus Penicillium, p. 316. In: Pitt JI (ed) The Genus Penicillium. Academic Press, London.
Raper KB, Thom C (1968) Chapter 8. Section Asymmetrica Raper and Thom. In: Raper KB, Thom C (ed) A manual of the Penicillia. The Williams and Wilkins, Baltimore, p 254.
Sugiura M (1984) Bacterial lipases. In: Borgström B, Brockman HL (eds) Lipases. Elsevier Science Publishers, Amsterdam, pp 505–523.
Tornqvist H, Belfrage P (1976) Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue. J Biol Chem 251:813–819.
Winkler FK, D'Arcy A, Hunziker W (1990) Structure of human pancreatic lipase. Nature 343:771–774.
Yokozeki K, Yamanaka S, Takinami K, Hirose Y, Tanaka A, Sonomoto K, Fukui S (1982) Application of immobilized lipase to regio-specific interesterification of triglyceride in organic solvent. Appl Microbiol Biotechnol 14:1–5.
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Yamaguchi, S., Mase, T. Purification and characterization of mono-and diacylglycerol lipase isolated from Penicillium camembertii U-150. Appl Microbiol Biotechnol 34, 720–725 (1991). https://doi.org/10.1007/BF00169340
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DOI: https://doi.org/10.1007/BF00169340