Purification of pregastric lipases of caprine origin

Lai, Douglas T., Stanley, Roger D. and O'Connor, Charmian J. (1998) Purification of pregastric lipases of caprine origin. Journal of the American Oil Chemists' Society, 75 3: 411-416. doi:10.1007/s11746-998-0060-5


Author Lai, Douglas T.
Stanley, Roger D.
O'Connor, Charmian J.
Title Purification of pregastric lipases of caprine origin
Journal name Journal of the American Oil Chemists' Society   Check publisher's open access policy
ISSN 0003-021X
1558-9331
Publication date 1998-03
Sub-type Article (original research)
DOI 10.1007/s11746-998-0060-5
Volume 75
Issue 3
Start page 411
End page 416
Total pages 5
Place of publication Heidelberg, Germany
Publisher Springer
Language eng
Abstract 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.
Keyword Albumin
Enzyme purification
Enzyme stability
Goat
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Agriculture and Food Sciences
Queensland Alliance for Agriculture and Food Innovation
 
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Created: Mon, 07 Mar 2011, 15:26:52 EST