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Studies on positional specificity of the castor bean acid lipase
Author(s) -
Ory Robert L.,
Kiser James,
Pradel Paul A.
Publication year - 1969
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02533183
Subject(s) - lipase , hydrolysis , chemistry , glyceride , fatty acid , lipolysis , organic chemistry , triolein , biochemistry , castor oil , tripalmitin , enzyme , adipose tissue
The acid lipase of castor bean endosperm catalyzed the hydrolysis of fatty acids from the 1 and 3 positions of synthetic glycerides immediately after achieving proper reaction conditions, but fatty acids from the 2 position were not detected in the reaction products until 7 to 10 min later. Results obtained with 2,3‐butane dioleate, n‐hexyl oleate and 2‐hexyl oleate showed that the castor lipase does not cleave secondary ester linkages. These findings suggest that the acid lipase of the castor bean may catalyze hydrolysis of fatty acids from the 1 and 3 positions of triglycerides only; the steady appearance of 2 position fatty acids in the reaction products during lipolysis is probably the result of an apparent isomerization reaction.