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Action of human pancreatic and salivary α-amylases on maltooligosaccharides: Evaluation of kinetic parameters

1979; Elsevier BV; Volume: 97; Issue: 2-3 Linguagem: Inglês

10.1016/0009-8981(79)90423-6

1873-3492

Narimasa Saito, Tatsuo Horiuchi, Mitsutaka Yoshida, Toshio Imai,

Microbial Metabolites in Food Biotechnology

The kinetic studies on the reactions of human pancreatic and salivary alpha-amylases with several maltooligosaccharides (maltotetraose, maltopentaose, maltohexaose, and maltoheptaose) were carried out. The susceptibility to hydrolysis with human pancreatic alpha-amylase decreased in the order of maltopentaose, maltohexaose, maltotetraose, and maltoheptaose, while with human salivary alpha-amylase maltopentaose was hydrolysed slightly slower than maltohexaose but fairly faster than maltotetraose or maltoheptaose from a viewpoint of the rates of reactions based on the amount of substrate changed. The relative rates of production of substrates, utilized in the coupled yeast alpha-glucosidase reaction, increased in the order of maltoheptaose, maltohexaose, maltotetraose, and maltopentaose with human pancreatic alpha-amylase, while with human salivary alpha-amylase in the order of maltoheptaose, maltotetraose, maltohexaose, and maltopentaose. Thus, maltopentaose was considered to be the best substrate over maltotetraose, maltohexaose or maltoheptaose for the alpha-glucosidase coupled method of alpha-amylase determination.