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Thermostable α-galactosidase from Bacillus stearothermophilus (NCIM 5146) and its application in the removal of flatulence causing factors from soymilk by Manoj Gote; Harshali Umalkar; Islam Khan; Jayant Khire is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Thermostable, neutral, extracellular ␣-galactosidase with wide pH stability was produced by a newly isolated strain of Bacillus stearother- mophilus (NCIM 5146) grown on cheap agricultural residues at 60 • C, under submerged fermentation conditions. The maximum ␣-galactosidase activity (2.0 U/ml) was found when soybean meal was used as a carbon source along with yeast extract and ammonium sulphate as a nitrogen source. The pH optimum of ␣-galactosidase was 6.5-7.0 and the enzyme was stable in the pH range of 3-10. The enzyme exhibited an optimum temperature of 65 • C. The half-life of the enzyme at 70 • C was 80 min. The enzyme was active against synthetic as well as natural substrates. The K m values determined for pNPG, stachyose, raffinose and melibiose were 0.625, 3.33, 6.66 and 13.33 mM, respectively. The V max values were 4.3 × 10 7 , 18.03, 12.65 and 6.3 × 10 3 mol/min mg, respectively, for the above substrates. Enzyme activity was strongly inhibited by Ag + , Hg 2+ and Cu 2+ metal salts. No significant inhibition was found in the presence of different sugars. The enzyme hydrolyzes flatulence causing galacto-oligosaccharides, viz. raffinose and stachyose present in the soymi

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Author

Manoj Gote; Harshali Umalkar; Islam Khan; Jayant Khire

Publisher

Elsevier Science; Elsevier ; Elsevier Applied Science; Elsevier BV (ISSN 1873-3298)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)