• The Korean Journal of Food And Nutrition
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• v.11 no.3
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• pp.319-322
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• 1998

The whole cell of alkalophilic Streptomyces sp. B-2 which produce glucose isomerase was immobilized by entrapment method for the effective production of high fructose syrup. The highest immobilized activity was achieved when the enzyme was bound to 2% $textsc{k}$-carrageenan. Immobilized glucose isomerase the pH optimum was about pH 7.5~8.5. Immobilization of alkalophilic Streptomyces sp. B-2 on 2% $textsc{k}$-carrageenan at 7$0^{\circ}C$ showed an increase in glucose isomerase activity. GI activity of immobilized cells was maximum Co2+ concentration 10-3M, Mg2+ concentration 10-3M.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.1
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• pp.35-39
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• 1997

Studies on the glucose isomerase produced by alkalophilic Streptomyces sp. B-2. Glucose Isomerase (E. C. 5.3.1.5) which reversibly catalyzes reaction between D-glucose and D-fructose was demonstrated in cell free extracts of alkalophilic Streptomyces sp. B-2 isolated form soil. The maximum enzyme activity was found at glucose concentration 4(g/$\ell$) , xylose concentration 6(g/$\ell$), magnesium ion 1.0(g/$\ell$), yeast extract concentration 2.0(g/$\ell$), peptone concentration 3(g/$\ell$).

• Journal of the East Asian Society of Dietary Life
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• v.10 no.5
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• pp.439-444
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• 2000

호알칼리성 방선균 Streptomyes sp. B-2를 Glucose Isomerse 생성을 위해 토양에서 분리했다. Glucose Isomerase(G.I)는 high fructose glucose syrup과 fructose의 생산을 위해서 식품 공업에서 아주 중요시되고 있는 효소이다. 호알칼리성 방선균 Streptomyces sp. B-2가 생성하는 glucose isomerase(G.I.)를 정제하였다. G.I.는 (NH$_4$)$_2$So$_4$분획, DEAE-cellulose, Sephadex G-200 chromatography하여 순수 분리 하였다. 순수분리된 G.I.는 electrophoresis에 의해 확인을 했다. SDS-acrylamide gel electrophoresis에 의해 정제된 효소는 single band를 보여주었다.

• The Korean Journal of Food And Nutrition
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• v.2 no.1
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• pp.1-11
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• 1989

Glucose isomerase (E.C.5.3.1.5) which reversibly catalyzes reaction between D-glucose and D-fructose was demonstrated in cell free extracts of alkalophilic Streptomyces sp. B-2 isolated from soil The optimum temperature, pH, and pH stability were 6$0^{\circ}C$, 10.5, and 7.8, respectively. The production of Gl in xylose and yeast extract was higher than that of other carbon source and nitrogen source. The Gl production was affected by Co2+ and Mg2).

• Microbiology and Biotechnology Letters
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• v.40 no.4
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• pp.303-309
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• 2012

Keratinases are of particular interest because of their action on insoluble keratins and generally on a broad range of protein substrates. Alkalophilic and neutrophilic actinomycete strains isolated from different soil samples, rich in keratinaceous substances were screened for keratinolytic activity. An alkalophilic isolate, TBG-S13A5, was found to possess good keratinolytic activity and was able to utilize feather as the sole carbon and nitrogen source. TBG-S13A5 exhibited an off-white aerial mass color with a rectus-flexibilis type of spore chain. The morphological, microscopical and biochemical characters were comparable with that of Streptomyces albidoflavus. Fatty acid methyl ester profiling (FAME) and 16S rDNA sequence analysis confirmed its identity as a strain of S. albidoflavus. Under submerged fermentation conditions, maximum protease production was recorded on the $5^{th}$ day of incubation at $30^{\circ}C$, using basal broth of pH 9.0 with 0.25% (w/v) white chicken feather. This strain could affect feather degradation when the initial pH was 8 and above and maximum protease production was recorded when the initial pH was around 10.5. The effectiveness of the crude enzyme in destaining and leather dehairing were also demonstrated.