Purification of pregastric lipases of caprine origin

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. JAOCS 75, 411-416 (1998).

Flavour development in dairy cream using fish digestive lipases from Chinook salmon (Oncorhynchus tshawytscha) and New Zealand hoki (Macruronus novaezealandiae)

“…Pregastric esterase (PGE), also called pregastric lipase or lingual lipase, is sourced from ruminants (calf, kid and lamb) and used for accelerated ripening and development of characteristic flavours in several cheeses and other dairy products (Birschbach, 1994;Hernández et al, 2009;Lai, Stanley, & O'Connor, 1998). This is due to the specificity, for short chain FA, of all the ruminant PGE enzymes (O'Connor, Bang, Taylor, & Brimble, 2001).…”

Partial Characterization of a Lipase from Gypsy Moth (Lymantria dispar L.) Larval Midgut

“…Lipases are widely distributed in nature and their physical and biochemical properties, and activities, have been investigated in many species of animals (GROENER & KNAUER 1981;LAI et al 1998;DEERLI & ALI AKPINAR 2002;OKU et al 2006), plants (LAMIKANRA & WATSON 2004;ZHONG & GLATZ 2006), bacteria (SIMONS et al 1996;HONG & CHANG 1998;DOSANJH & KAUR 2002;TEO et al 2003;GUPTA et al 2004), yeast (CRABBE et al 1996 and fungi (GARCIA-LEPE et al 1997;PAN-DEY et al 1999;PERA et al 2006). By using nitrophenyl esters as substrates, lipases have been investigated in bacteria (HUMBLE et al 1977;ARAGON et al 2000), insects (COSTA & DA CRUZ-LANDIM 2005), and other arthropods (GIB- SON & BARKER 1979;L[PEZ-L[PEZ et al 2003).…”

Synergistic Effects of Surfactants on Kid Pregastric Lipase Catalyzed Hydrolysis Reactions

“…Chemicals. Purification of kid pregastric lipase (PGL) from commercial extracts followed the procedure described previously . The specific activity was 533 μmol min -1 per mg of enzyme, for the catalyzed hydrolysis of 8.6 mM tributyrin in 1% lecithin emulsion at pH 6.5, 35 °C.…”

“…The work of Richardson and Nelson 2 did not clarify the debate on terminology, since the hydrolysis of esters or soluble triacetin may have also been due to the presence of an esterase in the enzyme preparation. There is clear evidence for the presence of esterase components in some pregastric lipase extracts, and their presence largely depends on the methods used for extraction. , The esterolytic component in the enzyme extracts showed those characteristics expected of an esterase, which only catalyzes the hydrolysis of water-soluble esters, e.g., p -nitrophenyl esters, but not monoacid triacylglycerols. , However, the purified lipolytic component in the pregastric extract was capable of catalyzing the hydrolysis of both soluble substrates and water-insoluble aggregates.…”