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PURIFICATION AND SOME PROPERTIES OF LIPASE FROM Streptococcus faecalis
Author(s) -
CHANDER HARISH,
RANGANATHAN B.,
SINGH JASJIT
Publication year - 1979
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1979.tb09131.x
Subject(s) - chemistry , chromatography , triolein , lipase , isoelectric point , tributyrin , size exclusion chromatography , sephadex , hydrolysis , triacylglycerol lipase , enzyme assay , fractionation , ammonium , enzyme , biochemistry , organic chemistry
Streptococcus faecalis possesses a glycerol ester hydrolase (lipase). The enzyme was purified from cell‐free extract by ammonium sulphate precipitation, Sephadex G‐25 filtration, acetone fractionation, Sephadex G‐75 filtration, ion exchange chromatography on DEAE cellulose, to 140‐fold with 30% recovery. The isoelectric point of enzyme was found to be 3.6. Its molecular weight was 20,900. With regards to amino acid content, glutamic acid was present in maximum amounts as compared to other amino acids, while cysteine was present in minimum amounts. Michaelis constant of lipase was 5.0 X 10 ‐3 M at pH 7.5 at 40°C. Of the simple triglycerides, tributyrin was hydrolyzed most easily by the enzyme, as compared to tricaproin, tricaprylin and triolein. The relative specificity of purified lipase for natural triglycerides was in the following order: butter oil > olive oil > linseed oil > coconut oil. Maximum enzyme activity with butter oil as substrate, was observed at pH 7.5 at 40°C. The enzyme was stable for 1 month at ‐18°C and was completely inactivated in 10 min at 90°C. The enzyme was stable at pH levels ranging from 6.0‐8.0. Addition of bile salts (0.2%) stimulated enzyme activities.