Premium
Reaction selectivity of Burkholderia cepacia (PS‐30) lipase as influenced by monoacylation of sn ‐glycerol
Author(s) -
Fu Xun,
Parkin Kirk L.
Publication year - 2004
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/s11746-004-0855-1
Subject(s) - selectivity , chemistry , lipase , burkholderia , glycerol , substrate (aquarium) , alcohol , oleic acid , organic chemistry , enzyme , bacteria , catalysis , biochemistry , biology , genetics , ecology
Reaction selectivities were determined in multicompetitive reactions mediated by Burkholderia cepacia lipase (Amano PS‐30) at a water activity of 0.19 in hexane. Saturated FA (C4–C18 even chain) and oleic acid (C18∶1) were reacted with a single alcohol, glycerol, α‐or β‐MAG, containing C4, C10, C16, or C18∶1 individually as alcohol cosubstrate. Similar odrinal patterns of FA selectivity, with C8, C10, and C16 preferred over others, were generally observed for incorporation of FA into specific acylglycerol (AG) pools of the 24 specific cases evaluated. The three exceptions were enrichment of C14 and C18 in the MAG pool with α‐C16‐MAG, substrate, and a general suppression of >C8 incorporation into the TAG pool for reactions with α‐C10‐ and α‐C16‐MAG. PS‐30 lipase selectivity toward MAG was in descending order: α/β‐C4‐MAG>β‐C10‐MAG>β‐C16‐MAG>α/β‐C18∶1‐MAG>α‐C10‐MAG>α‐C16‐MAG. Selectivity in channeling CX of the original CX‐MAG substrates into higher AG species was in descending order: α‐C10‐MAG∼α‐C16‐MAG>α‐C18∶1‐MAG>β‐C10‐MAG∼β‐C16‐MAG∼β‐C18∶1‐MAG >α/β‐C4‐MAG. Generally, MAG were better acyl donors than FA for esterification reactions leading to DAG formation. These observations are relevant to the design of biocatalytic processes intended to yield specifically structured TAG.