Abstract
The hydrolysis of malto-oligosaccharides G3-G6 catalysed by porcine pancreatic alpha-amylase was investigated kinetically at 25°. Kinetic parameters corresponding to different positions of enzymic attack were determined and product inhibition was evaluated. The enzymic hydrolysis was compared in terms of reaction rate and pattern of action with hydrolysis in 0.1m H2SO4 at 70°. Mathematical models for the mechanism of hydrolysis were developed and a good rationalisation of the experimental results was achieved.
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