Manuscript Abstract

XYLOSE ISOMERASES FROM THERMOTOGALES
B. Fatima, Z. Hussain

B. Fatima and Z. Hussain

Institute of Industrial Biotechnology (IIB), GC University Lahore, Kachery Road Lahore, 54000, Pakistan

Corresponding Author: fatima_gcu@yahoo.com
Page Number(s): 10-18
Published Online First: February 01, 2015
Publication Date: February 01, 2015
ABSTRACT

Biotechnology has been directed primarily towards reproductive technology been employed for improvement of
industrial important enzymes which are foremost concern over the years for researchers. This review paper discusses the
exciting scientific and technical advances in molecular biology for the genetic improvement in thermotogales, the
hyperthermophiles with respect to xylose isomerase to meet the industrial demands. A thermo-acid stable enzyme
possesses neutral or slightly acidic pH optima and a higher affinity for glucose have a potential for industrial applications
for the production of high fructose corn syrup (HFCS). Xylose isomerases from Thermotoga sp are class II enzymes,
utilize a 1, 2 hydride shift catalytic mechanism, active only in the presence of Mn+2, Co+2 and Mg+2
. Recombinant xylose
isomerases from T. neapolitana existed both as homodimer as well as homotetramer have been produced under
mesophilic fermentation conditions, with a maximal activity at 97°C. Mutant enzyme in addition to this catalytically
active at pH 5.5 and showed 3.1 fold increased catalytic efficiency towards glucose. The addition of the carbohydrate
biding domain to Thermotoga’s xylose isomerase successfully immobilized the enzyme to chitin beads. The turnover
numbers (kcat) for glucose to fructose conversion for both unbound and immobilized mutants was greater than the wildtype enzyme.

Keywords: xylose isomerases, thermotogales, hyperthermophiles
Open Access: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( https://creativecommons.org/licenses/by/4.0/).


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