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- W2076995781 abstract "Glycosylated α-galactosidase (melibiase) has been purified from white chickpea (Cicer arietinum) to 340-fold with a specific activity of 61 units/mg. Cicer α-galactosidase showed a Mr of 45 kDa on SDS-PAGE and by MALDI-TOF. The optimum pH and temperature with pNPGal were 4.5 and 50 °C, respectively. The Km for hydrolysis of pNPGal was 0.70 mM. Besides hydrolyzing the pNPGal, Cicer α-galactosidase also hydrolyzed natural substrates such as melibiose, raffinose, and stachyose very effectively; hence, it can be exploited commercially for improving the nutritional value of soy milk. Galactose was found to be a competitive inhibitor. The property of this enzyme to cleave the terminal galactose residues can be utilized for converting the group B erythrocytes to group O erythrocytes." @default.
- W2076995781 created "2016-06-24" @default.
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- W2076995781 date "2012-03-19" @default.
- W2076995781 modified "2023-10-14" @default.
- W2076995781 title "Purification and Characterization of α-Galactosidase from White Chickpea (Cicer arietinum)" @default.
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- W2076995781 doi "https://doi.org/10.1021/jf204538m" @default.
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