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Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae

Paper ID Volume ID Publish Year Pages File Format Full-Text
24476 43518 2010 7 PDF Available
Title
Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae
Abstract

In this work, a system for high-level secretion by Saccharomyces cerevisiae of the Thermus thermophilus HB27 putative esterase YP_004875.1 was constructed. The recombinant protein was purified and partially characterised. Its lipolytic activity dropped abruptly when the acyl chain length of the substrate increased from 12 to 18 carbon atoms, and variation of the reaction rate as function of substrate concentration followed Michaelis–Menten kinetics. These results suggested that the enzyme was an esterase. The recombinant enzyme was N-glycosylated and both the glycosylated and non-glycosylated forms showed activity. Compared to the native enzyme, thermal stability (half-life of 4.3 h at 85 °C) was higher, optimum temperature (40 °C) was lower and optimum pH (7.5–8.5) was similar. These characteristics support potential biotechnological applications of the recombinant esterase.

Keywords
Thermus thermophilus; Thermophilic esterase; Heterologous expression
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Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 145, Issue 3, 1 February 2010, Pages 226–232
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us