Literature DB >> 8072956

Immobilization of D-xylose (D-glucose) isomerase from a Chainia species.

H S Pawar1, D R Deshmukh.   

Abstract

D-Xylose isomerase is a heat-stable enzyme which isomerizes D-xylose into D-xylulose. D-Xylose isomerase from various species also isomerizes D-glucose into D-fructose. This enzyme is used in industry for the production of high-fructose corn syrup. The enzyme is specific for both, xylose and glucose. In most species xylose isomerase is localized intracellularly. However, in a rare actinomycete, Chainia sp. (NCL 82-5-1), xylose isomerase is present in both intracellular and extracellular compartments. We have previously purified and characterized intracellular enzyme from Chainia sp. In the present paper, we describe a procedure for immobilization of intracellular xylose isomerase on INDION 48-R by ionic binding. This method is inexpensive, does not require cross-linking agents and results in firm binding of the enzyme with the resin. The properties of immobilized enzyme such as pH optimum, substrate specificity, Km and inhibition by various metabolites are described and compared with those of purified, nonimmobilized enzyme.

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Year:  1994        PMID: 8072956     DOI: 10.1080/10826069408010088

Source DB:  PubMed          Journal:  Prep Biochem        ISSN: 0032-7484


  2 in total

1.  Optimization of Fermentation Medium for the Production of Glucose Isomerase Using Streptomyces sp. SB-P1.

Authors:  Sheetal Bhasin; H A Modi
Journal:  Biotechnol Res Int       Date:  2012-07-26

2.  Proteogenomic analysis of a thermophilic bacterial consortium adapted to deconstruct switchgrass.

Authors:  Patrik D'haeseleer; John M Gladden; Martin Allgaier; Patrik S G Chain; Susannah G Tringe; Stephanie A Malfatti; Joshua T Aldrich; Carrie D Nicora; Errol W Robinson; Ljiljana Paša-Tolić; Philip Hugenholtz; Blake A Simmons; Steven W Singer
Journal:  PLoS One       Date:  2013-07-19       Impact factor: 3.240

  2 in total

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