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Bioprocess Biosyst Eng. 2014 Jun;37(6):1211-9. doi: 10.1007/s00449-013-1093-1. Epub 2013 Dec 10.

Heterologous expression and biochemical characterization of glucose isomerase from Thermobifida fusca.

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1
State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Ave., Wuxi, 214122, People's Republic of China.

Abstract

Glucose isomerase (GIase) catalyzes the isomerization of D-glucose to D-fructose. The GIase from Thermobifida fusca WSH03-11 was expressed in Escherichia coli BL21(DE3), and the purified enzyme took the form of a tetramer in solution and displayed a pI value of 5.05. The temperature optimum of GIase was 80 °C and its half life was about 2 h at 80 °C or 15 h at 70 °C. The pH optimum of GIase was 10 and the enzyme retained 95 % activity over the pH range of 5-10 after incubating at 4 °C for 24 h. Kinetic studies showed that the K m and K cat values of the enzyme are 197 mM and 1,688 min(-1), respectively. The maximum conversion yield of glucose (45 %, w/v) to fructose of the enzyme was 53 % at pH 7.5 and 70 °C. The present study provides the basis for the industrial application of recombinant T. fusca GIase in the production of high fructose syrup.

PMID:
24317483
DOI:
10.1007/s00449-013-1093-1
[Indexed for MEDLINE]
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