Partial purification and properties of .beta.-amylase isolated from Sorghum bicolor (L.) Moench

• Published in: Journal of agricultural and food chemistry Vol. 32; no. 1; pp. 11 - 14
• Main Authors: Okon, Ekong U, Uwaifo, Anthony O
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.01.1984
• Subjects: beta -amylase; Biological and medical sciences; Cereal and baking product industries; Food industries; Fundamental and applied biological sciences. Psychology; Sorghum bicolor; Sorghum; Fractionation; Enzymatic activity; Amylase; Enzyme
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf00121a003

beta -Amylase was extracted from Sorghum bicolor (L.) Moench variety L. 187 and purified by ammonium sulfate fractionation followed by gel filtration on Sephadex G-200. The yield of beta -amylase activity in the final purification was 54% of the original activity and specific activity was increased approximately 5-fold. Three components were separated with molecular weights of 20,000, 40,000, and 80,000 based on the selectivity curve for the Sephadex column determined with standard proteins. All components were enzymatically active. The enzyme had a pH optimum of 5.0-5.5 and an energy of activation of 57.48 J mol super(-1) between 10 and 40 degree C. The calculated V sub(max) and K sub(m) values for the enzyme were 7.466 x 10 super(-3) enzyme units and 1,272 g of starch/L, respectively.