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HYDROLYTIC SELECTIVITY OF PATATIN (LIPID ACYL HYDROLASE) FROM POTATO ( SOLANUM TUBEROSUM L.) TUBERS TOWARD VARIOUS LIPIDS
Author(s) -
ANDERSON COREY,
PINSIRODOM PRAPHAN,
PARKIN KIRK L.
Publication year - 2002
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2002.tb00050.x
Subject(s) - chemistry , phospholipid , glyceride , hydrolysis , hydrolase , enzyme , biochemistry , substrate (aquarium) , selectivity , fatty acid , solanum tuberosum , lipase , stereochemistry , biology , catalysis , ecology , membrane , horticulture
The fatty acid and positional hydrolytic selectivity of lipid acyl hydrolase (LAH; patatin) isolated from potato tubers was determined for acylgfycerol and phospholipid substrates. LAH was about 3‐fold more selective for decanoyl residues over other acyl groups of 8–18 carbons for partial glyceride substrates. For both mono‐ and diacylglycerols, LAH preferred substrates with primary (sn‐1 (3)‐) ester linkages, indicating a regiobias for these sites over sn‐2‐linked acyl groups. Similarly, hydrolytic activity on phospholipid substrates was 5‐ to 10‐fold faster on sn‐l‐palmitoyl, sn‐2‐lysophospholipids than on intact phospholipids, indicating a preference for either lysophospholipids or sn‐l‐acyl sites, or both. LAH activity on partial glycerides was not activated by CaCl 2 and had a greater temperature optimum relative to LAH activity on phospholipid substrates. These differences are likely based on differences in forces and structural features conferring enzyme‐substrate recognition for these substrates within a common active site.