Porcine pancreatic α-amylase was separated on DEAE-cellulose into two isoforms, i.e., PPA-I and PPA-II and their molecular weight was found to be ∼ 55 kDa by gel filtration. The pH and temperature optima of PPA and its isoforms were 6.9 and 45°C. Chlorides of metal ions Ca2+, Ba2+, Co2+, and Mg2+ enhanced the enzyme activity, whereas Al3+ and Hg2+ completely inactivated the enzyme. Oxalic and citric acids inhibition of PPA and its isoforms is concentration dependant. EDTA was found to be the most effective inhibitor. PPA and its isoforms released maltotriose and maltotetraose from starches.
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Gopal et al. (2009) studied this question.
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