Identification of an acidic alpha-amylase from Alicyclobacillus sp A4 and assessment of its application in the starch industry

作者：Bai, Yingguo; Huang, Huoqing; Meng, Kun; Shi, Pengjun; Yang, Peilong; Luo, Huiying; Luo, Chunliang; Feng, Yukun; Zhang, Wei^*; Yao, Bin

来源：Food Chemistry, 2012, 131(4): 1473-1478.

DOI：10.1016/j.foodchem.2011.10.036

• Alicyclobacillus sp A4
• Acidic alpha-amylase
• Raw starch digesting enzyme

An acidic alpha-amylase was purified from thermoacidophilic Alicyclobacillus sp. A4 by ion exchange chromatography with 22% recovery, and showed a molecular mass of 64 kDa by SOS-PAGE. Its amino acid sequence was determined by sequencing three internal peptides and the complete genome of strain A4, and shared highest identity (64%) with Alicyclobacillus acidocaldarius alpha-amylase. Compared with other reported alpha-amylases, the purified enzyme had some distinct characteristics. The optimal activity was found to occur at 75 degrees C and pH 4.2, similar to the glucamylase widely used in the starch industry. The enzyme was Ca2+ independent, and had strong ability to digest raw starch (96.71%) with commercial glucamylase in one step. These properties of the purified enzyme make up the deficiency of the commercial alpha-amylases currently used and avoid repeated adjustment of pH and temperature in double-enzymatic sugar-making process. The purified enzyme will be commercially valuable in the starch industry.

• 出版日期2012-4-15
• 单位中国农业科学院