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Purification of pregastric lipases of caprine origin
Author(s) -
Lai Douglas T.,
Stanley Roger D.,
O’Connor Charmian J.
Publication year - 1998
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/s11746-998-0060-5
Subject(s) - chemistry , chromatography , lecithin , albumin , casein , emulsion , polyacrylamide gel electrophoresis , sodium dodecyl sulfate , enzyme , electrophoresis , lipase , substrate (aquarium) , sodium , glycerol , biochemistry , biology , ecology , organic chemistry
Pregastric lipases from kid (KPGL) and goat (GPGL) were purified from the commercial extracts by different chromatographic procedures. The total recovery of activity for both purification methods was ca . 10%, and the specific activities of KPGL and GPGL were 533 and 546 U/mg, respectively, at pH 6.5, 35°C for tributyrylglycerol (TBG) as substrate in a casein/lecithin emulsion. The purification factors were 130‐ and 76‐fold for the goat and kid lipases, respectively. The purified lipases from kid and goat showed the same 50 kDa protein band on sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and an identical sequence for the first 11 amino acids. The optimal pH for the lipases was within the pH range 6–7, with maximal activity at pH 6.5. The stability of the purified lipases was decreased dramatically at pH>6.5, but was enhanced by the addition of albumin.