Cold-active extracellular lipase: Expression in Sf9 insect cells, purification, and catalysis.

ABSTRACT: Cold-active lipases are gaining special attention nowadays as they are increasingly used in various industries such as fine chemical synthesis, food processing, and washer detergent. In the present study, an extracellular lipase gene from Yarrowia lipolytica (LIPY8) was cloned and expressed by baculovirus expression system. The recombinant lipase (LipY8p) was purified using chromatographic techniques, resulting in a purification factor of 25.7-fold with a specific activity of 1102.9U/mg toward olive oil. The apparent molecular mass of purified LipY8p was 40 kDa. The enzyme was most active at pH 7.5 and 17 °C. It exhibited maximum activity toward medium chain (C10) esters. The presence of transition metals such as Zn²⁺, Cu²⁺, and Ni²⁺ strongly

SUBMITTER: Li T 

PROVIDER: S-EPMC6290134 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature