Subsite Affinities of β-Glucosidase from Aspergillus sojae on Various Xylooligosaccharides
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概要
- 論文の詳細を見る
The subsite affinities of β-glucosidase(EC 3.2.1.21)with high β-xylosidase activity from Aspergillus sojae on various xylooligosaccharides(degree of polymerization : n=2-6)were investigated by steady-state kinetic analysis. The molecular activity(k_0)value of the enzyme for xylobiose was not markedly different from those of other substrates(n=3-6). The arrangement of the subsite affinities(A_i, i=1-6)was evaluated ; A_1=2.93 kcal/mol, A_2=3.67 kcal/mol, A_3=0.64 kcal/mol, A_4=0.12 kcal/mol, A_5=-0.07 kcal/mol, A_6=-0.05 kcal/mol, and the intrinsic rate constant(k_<int>)was 7.6s^<-1>. The subsite structure was similar to those of β-glucosidase from A.niger and α-glucosidases from A.niger and Mucor javanicus, where the values for A_1 were much larger than those for A_3.
- 社団法人日本生物工学会の論文
- 1999-05-25
著者
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Tajima Shigeyuki
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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KIMURA Isao
Kagawa Prefectural Industrial Center
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Tajima Shigeyuki
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Tajima Shigeyuki
Department Of Agricultural Chemistry Faculty Of Agriculture Nagoya University
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Kimura Isao
Kagawa Prefectural Fermentation And Food Experimental Station
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