Asparaginase specifically catalyzes the hydrolysis of amide bond of
asparagine to product aspartic acid. During the processing of starch-rich food
at high temperature acrylamide is usually produced. Acrylamide is thought to be
a potential carcinogen. Asparaginase is able to degrade the precursor of
acrylamide, asparagine, to prevent the formation of acrylamide, and thus greatly reduces the acrylamide level in final
product.
Asparaginase
can reduce the content of asparagine in the raw material by converting it to
aspartic acid, which undergoes a Maillard reaction instead. In this way, acrylamide
will not be generated afterwards. So, the use of asparaginase can reduce the
production of acrylamide in food, but it will not affect the appearance, taste
and flavor of the product.