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Expression and activity analysis of sucrose:sucrose 1-fructosyltransferase from onion

Paper ID Volume ID Publish Year Pages File Format Full-Text
33823 44992 2010 6 PDF Available
Title
Expression and activity analysis of sucrose:sucrose 1-fructosyltransferase from onion
Abstract

This study was designed to express the onion fructosyltransferase by Escherichia coli DH5α, and obtain the optimal conditions of FST-1 activity. Thereby, fructosyltransferase gene was obtained by RT-PCR from onion in this experiment, and named FST-1. The expressed proteins were analyzed by SDS-PAGE. FST-1 activity was identified by the high performance liquid chromatography (HPLC). The optimal conditions of FST-1 were analyzed by the dinonylnaphthalene sulfonic acid (DNS) and orthogonal test. Results revealed that FST-1 was identified to 98% similarity with fructosyltransferase mRNA of onion (accession number: AJ006066). FST-1 was successfully expressed in E. coli DH5α. HPLC results indicated that the expressed protein from FST-1 had a good transferring activity for fructose. The optimal conditions of FST-1 in catalyzing reaction were the pH 5.0, 45 °C and 60% sucrose substrate. The results in this experiment would lay the foundation for the large-scale of kestose by bio-catalysis method.

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Expression and activity analysis of sucrose:sucrose 1-fructosyltransferase from onion
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 27, Issue 4, 30 September 2010, Pages 324–329
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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