N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase.

ABSTRACT:

Background

Lipolytic enzymes of hyperthermophilic archaea generally prefer small carbon chain fatty acid esters (C₂-C₁₂) and are categorized as esterases. However, a few have shown activity with long-chain fatty acid esters, but none of them have been classified as a true lipase except a lipolytic enzyme AFL from Archaeglobus fulgidus. Thus, our main objective is to engineer an archaeal esterase into a true thermostable lipase for industrial applications. Lipases which hydrolyze long-chain fatty acid esters display an interfacial activation mediated by the lid domain which lies over active site and switches to open conformation at the oil-water interface. Lid domains modulate enzyme activities, substrate specificities, and stabilities which have been sh

SUBMITTER: Soni S 

PROVIDER: S-EPMC6501381 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature