Protein engineering of bacterial α-amylases

By Jens Erik Nielsen, T. Borchert. 2000

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A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104 (2005, background): “For example, -amylases used in tarch industry must be active and stable at low pH but in etergent industry at high pH values [7,8].”
An overview of the microbial α-amylase family (2003, background): “Engineering α-amylase for changed pH activity profiles also would add to the stability of the enzymes (Nielsen and Borchert, 2000). van der Maarel et al. (2000) and Gupta et al. (2003) have discussed extensively about the industrial applications of α-amylase family members.”
The determinants of α-amylase pH–activity profiles (2001, background): “Several of these processes take place at pH values which are very different from those where the α-amylases perform optimally ( Nielsen and Borchert, 2000 ) and consequently there is great interest in changing the pH–performance profile of the α-amylases (Nielsen et al., 1999a; Shaw et al., 1999) an”
Properties and applications of starch-converting enzymes of the alpha-amylase family. (2002, background): “Nielsen and Borchert (2000) have recently published a comprehensive overview of a number of experiments that have been done to engineer pH–activity proﬁles.”