Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/117981
Title: Production and characterization of glucose isomerase from Streptomyces lividans RSU26
Researcher: R. Sathya
Guide(s): Dr. T. Ushadevi
Keywords: Microbiology
University: Prist University
Completed Date: 22/10/2015
Abstract: Glucose isomerase (GI) is an intracellular enzyme that catalyzes the reversible isomerization of glucose to fructose, which is used in the manufacture of high fructose syrup in soft drinks. Many reports have been published about the importance of GI and its characteristics. However, improved characteristics of GI from microbial sources are therefore expected to fulfill the requirements of industrial applications. This study aimed at finding such an enzyme with improved glucose isomerase activity from natural resources. As marine Streptomyces are the rich sources of many industrial enzymes, this study was focused on isolating new Streptomyces which harbor novel GIs. Totally 151 strains isolated from mangrove soil. Morphologically distinct 56 isolates were selected for primary screening of GI. Among 56 isolates, 8 isolates have been identified to have good GI activity. The strains were further characterized biochemically and screened for glucose isomerase activities. The potent GI producing Streptomyces were identified by 16S rRNA sequencing and constructed phylogenetic alignment on sequence similarity basis. Based on screening, Sreptomyces lividans RSU26 was selected to work further to understand its growth and enzyme characteristics as it showed promising glucose isomerase activity, compared to other seven isolates. The culture conditions were optimized for the strain RSU26 and glucose isomerase was purified to the homogeneity and characterized for its activities. The purified GI RSU26 showed 43 kDa protein on an SDS-PAGE, while on native PAGE, it was newline170 kDa, suggesting a homo-tetrameric nature of the protein, as described previously. The Km for fructose was at 48.8 mM, while glucose had low Km at 29.4 mM. The Vmax of purified glucose isomerase RSU26 exhibited 2.54 and 2.38 U mg 1 protein, for its fructose and#61614; glucose, and glucose and#61614; fructose isomerization reactions, respectively at pH 7.5, temperature 50 and 65 oC. The catalytic efficiency (K
Pagination: A4
URI: http://hdl.handle.net/10603/117981
Appears in Departments:Department Of Microbiology

Files in This Item:
File Description SizeFormat 
acknowlegdements.pdfAttached File123.36 kBAdobe PDFView/Open
certificates.pdf145.41 kBAdobe PDFView/Open
chapter 1.pdf208.43 kBAdobe PDFView/Open
chapter 2.pdf313.95 kBAdobe PDFView/Open
chapter 3.pdf2.42 MBAdobe PDFView/Open
chapter 4.pdf435.62 kBAdobe PDFView/Open
chapter 5.pdf660.38 kBAdobe PDFView/Open
chapter 6.pdf143.38 kBAdobe PDFView/Open
contents.pdf143.42 kBAdobe PDFView/Open
list of tables figures.pdf138.96 kBAdobe PDFView/Open
references.pdf410.52 kBAdobe PDFView/Open
title.pdf109.07 kBAdobe PDFView/Open


Items in Shodhganga are protected by copyright, with all rights reserved, unless otherwise indicated.

Altmetric Badge: