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Article

Biochemical characterization and mutational improvement of a thermophilic esterase from Sulfolobus solfataricus P2.

Biotechnology letters - 1 Aug 2010

Shang Yu-Shuan, Zhang Xian-En, Wang Xu-De, Guo Yong-Chao, Zhang Zhi-Ping, Zhou Ya-Feng

Abstract excerpt

A thermophilic esterase, SsoPEst, from Sulfolobus solfataricus P2 was cloned and expressed in E. coli AD494 (DE3). Gene sequencing indicated the encoded 353 amino acids had less than 32% identity with reported esterases. The recombinant enzyme hydrolyzed p-nitrophenyl esters but not tributyrin or tricaprylin, exhibiting the highest specific activity (1.1 U/mg) with p-nitrophenyl caprylate. The enzyme was...

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PMID: 20386955
DOI: 10.1007/s10529-010-0274-0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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