Hydrolysis Activity of ${\alpha}-Galactosidase$ from Bacillus licheniformis

The maximum productivity of capable of hydrolyzing completely linkages within oligomeric substrates such as melibiose, raffinose and stachyose to liberate galactose residue, was reached to 718 mU/ml in the culture filtrate of Bacillus licheniformis at death phase. The was identified to show different efficiencies for hydrolyzing the according to analysis of reaction products by both TLC and quantification of the liberated reducing sugars. The enzyme was active on in the order of melibiose, raffinose, and stachyose. Though the hydrolyzing activity of enzyme was faintly inhibited by reaction products such as galactose, glucose and sucrose with amounts of five folds more than the added substrates (20 mM), the largest inhibition of enzyme activity was caused by galactose among the end products. Unknown compound, which migrated slower than melibiose on TLC, was detected during hydrolysis reaction of melibiose, suggesting that the has a glycosyl transferase activity. In addition, the enzyme was able to hydrolyze efficiently raffinose and stachyose existed in the soluble extract of soybean meal.