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Studies on free and immobilized lipases from Mucor miehei
Author(s) -
HugeJensen Birgitte,
Galluzzo Donna Rubano,
Jensen Robert G.
Publication year - 1988
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02544508
Subject(s) - lipase , chemistry , isoelectric point , rhizomucor miehei , hydrolysis , chromatography , substrate (aquarium) , enzyme , triacylglycerol lipase , biochemistry , biology , ecology
An extracellular lipase produced by fermentation with a selected strain of Mucor miehei has been purified partially in two forms: A and B. The forms have a high degree of antigenic identity and have similar pH‐activity profiles with tributyroylglycerol as the substrate with optima at pH 7. The differences are A, in contrast to B, requires activation at alkaline pH before analysis; A binds with concanavalin A more completely than B, the net charges are slightly different at pH 8; the isoelectric points are different. Our results indicate that the B lipase is formed by partial deglycosylation of the A lipase and that this influences the activity toward emulsions. The two enzymes have been immobilized by adsorption. These preparations and the soluble forms were highly specific for primary ester of triacylglycerols (TG), usually hydrolyzed TG of 12:0, 14:0, 16:0 and 18:1 more rapidly than those of 4:0, 6:0, 8:0 and 10:0 in mixtures of monoacid TG (4:0 to 18:1), and were not stereospecific for TG. Immobilization altered the specificity of the preparations somewhat in that slightly more 14:0 and 16:0 were released.