When alpha-amylase cleaves the glycosidic linkage in the blocked substrate, any other enzymes in the extract do not accelerate the hydrolysis to give free p-nitrophenol. The reason for this is that the level of thermostable alpha-glucosidase in the substrate mixture is saturating.
After alpha-amylase cleaves the internal glycosidic linkage of the Ceralpha substrate can beta-amylase or glucoamylase accelerate the hydrolysis reaction of the released p-nitrophenyl maltosaccharide?
Modified on: Wed, 30 Mar, 2016 at 9:56 AM
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