Cloning, Expression and Characterization of a Thermostable Esterase HydS14 from Actinomadura sp. Strain S14 in Pichia pastoris

Cloning, Expression and Characterization of a Thermostable Esterase HydS14 from Actinomadura sp. Strain S14 in Pichia pastoris

A thermostable esterase gene (hydS14) was cloned from an Actinomadura sp. S14 gene library. The gene is 777 bp in length and encodes a polypeptide of 258 amino acid residues with no signal peptide, no N-glycosylation site and a predicted molecular mass of 26,604 Da. The encoded protein contains the...

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Bibliographic Details
Main Authors: Pichapak Sriyapai, Fusako Kawai, Somjai Siripoke, Kosum Chansiri, Thayat Sriyapai
Format: Article
Language:English
Published: MDPI AG 2015-06-01
Series:International Journal of Molecular Sciences
Subjects:
Actinomadura sp.
esterase
α/β-hydrolase superfamily
lipolytic family
thermophile
Online Access:http://www.mdpi.com/1422-0067/16/6/13579

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http://www.mdpi.com/1422-0067/16/6/13579

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