title: Action of human pancreatic and salivary alpha-amylases on maltooligosaccharides: evaluation of kinetic parameters.
abstract: 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.
mesh_terms: D000328:Adult; D000681:Amylases / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008320:Maltose; D009844:Oligosaccharides / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D010306:Parotid Gland; D012463:Saliva / Q000201:enzymology*; D013379:Substrate Specificity; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D009844:Oligosaccharides; D008320:Maltose; D000681:Amylases; D000520:alpha-Glucosidases