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Characterization of sterol glucosyltransferase from Salinispora tropica CNB-440: Potential enzyme for the biosynthesis of sitosteryl glucoside

Paper ID Volume ID Publish Year Pages File Format Full-Text
17366 42663 2013 7 PDF Available
Title
Characterization of sterol glucosyltransferase from Salinispora tropica CNB-440: Potential enzyme for the biosynthesis of sitosteryl glucoside
Abstract

A sterol glucosyltransferase-encoded gene was isolated from Salinispora tropica CNB-440, a marine, sediment-dwelling, Gram positive bacterium that produces the potent anticancer compound, salinosporamide A. The full-length gene consists of 1284 nucleotides and encodes 427 amino acids with a calculated mass of 45.65 kDa. The gene was then cloned and heterologously expressed in Escherichia coli BL21(DE3). The amino acid sequence shares 39% similarity with the glycosyltransferase from Withania somnifera, which belongs to glycosyltransferase family 1. Enzyme reactions were carried out with the various free sterols (acceptor) and NDP-sugars (donor). The purified protein only showed activity for glucosylation of β-sitosterol with UDP-D-glucose and TDP-D-glucose donors, and optimal activity at pH 7.5 and 37 °C. Among these two donors, UDP-D-glucose was preferred.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► A sterol glucosyltransferase gene was isolated from Salinispora tropica CNB-440. ► Phylogenetic relationship analysis based on the C-terminal amino acid sequences. ► Heterologous expression successfully in E. coli BL21(DE3) and purified the protein. ► Biochemical properties were characterized and compared with another published reports.

Keywords
Biosynthesis; Salinisporatropica CNB-440; Sitosterylglucoside; Sterol glucosyltransferase
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Characterization of sterol glucosyltransferase from Salinispora tropica CNB-440: Potential enzyme for the biosynthesis of sitosteryl glucoside
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 52, Issues 4–5, 10 April 2013, Pages 234–240
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
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us