Abstract
A bacterium producing <TEX>${\alpha}$</TEX>-galactosidase (<TEX>${\alpha}$</TEX>-<TEX>$\small{D}$</TEX>-galactoside galactohydrolase, EC 3.2.1.22) was isolated. The isolate, KM-1 was identified as Bacillus coagulans based on its 16S rRNA sequence, morphology, and biochemical properties. <TEX>${\alpha}$</TEX>-Galactosidase activity was detected the culture supernatant of B. coagulans KM-1. The bacterium showed the maximum activity for hydrolyzing para-nitrophenyl-<TEX>${\alpha}$</TEX>-<TEX>$\small{D}$</TEX>-galactopyranoside (pNP-<TEX>${\alpha}Gal$</TEX>) at pH 6.0 and <TEX>$50^{\circ}C$</TEX>. It hydrolyzed oligomeric substrates such as melibiose, raffinose, and stachyose liberating a galactose residue, indicating that the B. coagulans KM-1 <TEX>${\alpha}$</TEX>-galactosidase hydrolyzed <TEX>${\alpha}$</TEX>-1,6 linkage. The results suggest that the decreased stachyose and raffinose contents in fermented soybean meal are due to the <TEX>${\alpha}$</TEX>-galactosidase activity.
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