Abstract
A new calcium independent α-amylase has been developed for starch liquefaction. This amylase Termamyl LCTM gives the same performance in the absence of free calcium compared to TermamylTM, in the presence of 40 ppm free calcium. The improvement is a result of 5 single amino acid substitutions and one N-terminal alteration. Several new alkaline α-amylases were identified in Nature. We have isolated two amylases that display the desired activity profile but lack the overall stability necessary for a detergent a-amylase. A two amino acid deletion in the region from position 180-184 increased the overall stability both with respect to temperature and calcium sensitivity, to a satisfactory level comparable to that of TermamylTM.
