An insight into ameliorating production, catalytic efficiency, thermostability and starch saccharification of acid-stable α-amylases from acidophiles

Abstract

Most of the extracellular enzymes of acidophilic bacteria and archaea are stable at acidic pH with a relatively high thermostability. There is, however, a dearth of information on their acid stability. Although several theories have been postulated, the adaptation of acidophilic proteins to low pH has not been explained convincingly. This review highlights recent developments in understanding the structure and biochemical characteristics, and production of acid-stable and calcium-independent a-amylases by acidophilic bacteria with special reference to that of Bacillus acidicola.