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Purification of pregastric lipases of caprine origin

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Journal of the American Oil Chemists' Society

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.

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Authors and Affiliations

  1. Department of Chemistry, The University of Auckland, PB 92019, Auckland, New Zealand

    Douglas T. Lai & Charmian J. O’Connor

  2. New Zealand Horticulture and Food Research Institute, Auckland, New Zealand

    Roger D. Stanley

Authors
  1. Douglas T. Lai
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  2. Roger D. Stanley
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  3. Charmian J. O’Connor
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Correspondence to Charmian J. O’Connor.

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Lai, D.T., Stanley, R.D. & O’Connor, C.J. Purification of pregastric lipases of caprine origin. J Amer Oil Chem Soc 75, 411–416 (1998). https://doi.org/10.1007/s11746-998-0060-5

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  • DOI: https://doi.org/10.1007/s11746-998-0060-5

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