Reaction selectivity of rhizomucor miehei lipase as influenced by monoacylation of sn-glycerol

Reaction selectivities were determined in multicompetitive reactions mediated by Rhizomucor miehei (RM) lipase at 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, or α-or β-MAG containing C4, C10, C16, or C18∶1 individually as alcohol cosubstrate. Similar patterns of broad FA selectivity toward C8–C18 FA were generally observed for esterification into specific acylglycerol (AG) pools with the different α/β-CX-MAG cosubstrates. Exceptions were enrichment of C18 in the MAG pool with α-C16-MAG substrate, and a general suppression of C4/C6 FA reactivity and a specific discrimination toward >C8 FA incorporation into the TAG pool, both for reactions with α-C10- and α-C16-MAG. RM lipase selectivity toward MAG was in descending order: β-C18∶1-MAG>α/β-C4-MAG∼β-C10-MAG∼β-C16-MAG>α-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>β-C10-MAGβ-C16-MAG>α-C18∶1-MAG>β-C18∶1-MAG∼ α/β-C4-MAG. Aside from their characteristic FA selectivity, Burkholderia cepacia (PS-30) and RM lipases behaved similarly in terms of MAG selectivity as well as a general conservation of FA selectivity throughout the sequential steps of TAG assembly from FA and glycerol for processes designed to yield specifically structured TAG.