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KMID : 0903519980410070489
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1998 Volume.41 No. 7 p.489 ~ p.495
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Characteristics and Action Pattern of α-galactosidase from Scopulariopsis brevicaulis in Korean Traditional Meju
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이희덕/Lee, Hee Duck
홍승표/최광수/이선호/최청/배두경/Hong, Seung Pyo/Choi, Kwang Soo/Lee, Seon Ho/Choi, Choeng/Bae, Du Kyung
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Abstract
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The optimum culture condition of Scopulariopsis brevicaulis for the production of α-galactosidase was as follows: Tryptone 1.5%, NH₄NO₃ 0.2%, Raffinose 2.5%, KH₂PO₄ 0.5%, yeast extract 0.5%, pH 7.0, 27℃. The optimum pH and temperature for the enzyme activity of α-galactosidase producing Scopulariopsis brevicaulis were pH 7.0 and 27℃, respectively. The enzyme was relatively stable at pH 6.0∼8.0 and at temperature below 40℃. The activity of the enzyme was inhibited by Ag^(2+), Hg^(2+), Cu^(2+), ρ-chloromercuribenzoic acid and Iodine. These results would indicate the presence of -SH groups in the catalytic site of the enzyme. Km value was 1.9 mM for ρ-nitrophenyl-α-D-galactopyranoside and Vmax value was 9.66 × 10² μM/min. Sugar constituents of culture broth were identified by HPLC that the enzyme liberated sucrose, glucose and fructose from raffinose and raffinose was significantly decreased.
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