Abstract

A novel lipase gene (lip4346) encoding a primary translation product with 176 amino acids was screened from the genome fine mapping of the macroalgae-associated bacterial strain Microbulbifer sp. YNDZ01. Macroalgae were collected from the coast of the Halmahera Island of Indonesia. The lip4346 gene was cloned and heterologously expressed in Escherichia coli. The purified recombinant Lip4346 protein had a molecular mass of 19kDa, a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and a maximum enzyme activity of 31.2UmL−1. The optimal temperature and pH for the lipase activity of Lip4346 were 70°C and 10.0, respectively. Lip4346 was tolerant with a number of organic solvents and detergents, and was active toward triacylglycerols and p-nitrophenyl esters with short- and medium-chain lengths. The unique characteristics of Lip4346 indicate that it is a promising nonaqueous biocatalyst for industrial applications.

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