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Purification and characterization of a lipase from Neurospora sp. TT‐241
Author(s) -
Lin Shuenfuh,
Lee JaneChyi,
Chiou ChienMing
Publication year - 1996
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02517950
Subject(s) - chemistry , diisopropyl fluorophosphate , triolein , lipase , sodium dodecyl sulfate , chromatography , glycerol , residue (chemistry) , polyacrylamide gel electrophoresis , solvent , organic chemistry , enzyme
An extracellular lipase, which is produced by the Neurospora sp. TT‐241 strain, grown on wheat bran at 30°C for 4 d, was purified 370‐fold with an overall yield of 16%. The molecular weight was determined to be 55 kDa by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. The optimal pH at 30°C and optimal temperature at pH 6.5 were 7 and 45°C, respectively. The lipase was stable in the pH range of 5 to 8, and it was temperature‐sensitive. It was active on a wide range of natural substrates of either vegetable or animal origins and toward p ‐nitrophenyl esters, greatly favoring those containing C 4 acyl groups. It cleaved all of the ester bonds of triolein; however, the 1‐ or 3‐ester bond was the preferred target. A complete inhibition by diisopropyl fluorophosphate suggested the presence of a serine residue at the active site. Partial inhibition was shown by either Hg 2+ or chloramine T. Enzyme activity persisted in nonionic surfactants, a water‐miscible solvent (dimethylsulfoxide), and a water‐immiscible solvent (hexane).