Reactivity of sorbose dehydrogenase from Sinorhizobium sp. 97507 for 1,5-anhydro-d-glucitol

Purified recombinant sorbose dehydrogenase from Sinorhizobium sp. 97507 exhibited high reactivity for 1,5-anhydro-d-glucitol (1,5-AG) and l-sorbose, but little activity for the other sugars or sugar alcohols tested. Kinetic analysis revealed that its catalytic efficiency (k cat /K m ) for l-sorbose...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2015-07, Vol.79 (7), p.1130-1132
Hauptverfasser:	Araki, Toshio, Nakatsuka, Tomoko, Kobayashi, Fuminao, Watanabe-Ishimaru, Emi, Sanada, Hirokazu, Tamura, Takashi, Inagaki, Kenji
Format:	Artikel
Sprache:	eng
Schlagworte:	1,5-anhydro-d-glucitol Bacterial Proteins - chemistry Bacterial Proteins - metabolism Carbohydrate Dehydrogenases - chemistry Carbohydrate Dehydrogenases - metabolism Deoxyglucose - metabolism Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sinorhizobium - enzymology Sinorhizobium - genetics Sinorhizobium sp Sorbose - metabolism sorbose dehydrogenase Substrate Specificity
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Zusammenfassung:	Purified recombinant sorbose dehydrogenase from Sinorhizobium sp. 97507 exhibited high reactivity for 1,5-anhydro-d-glucitol (1,5-AG) and l-sorbose, but little activity for the other sugars or sugar alcohols tested. Kinetic analysis revealed that its catalytic efficiency (k cat /K m ) for l-sorbose and 1,5-AG is 1.8 × 10 2 and 1.5 × 10 2 s −1 ·M −1 , respectively.
ISSN:	0916-8451 1347-6947
DOI:	10.1080/09168451.2015.1012148