DOI: 10.31274/rtd-180816-1078
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Action patterns of some alpha-type amylases

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Cited by 3 publications
(3 citation statements)
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“…For trypsin and chymotrypsin, one unit of enzyme activity (U) was defined as the amount of enzyme that released 1 µmol of p-nitroanilide per min, using 8800 M cm −1 as the extinction coefficient, measured at 405 nm. The amylase activity was determined according to the Somogyi-Nelson method using soluble starch (2% w/v) as the substrate, as described by Robyt and Whelan [33]. One unit of activity (U) was defined as the amount of enzyme capable of producing 1 mg of maltose per minute.…”
Section: Digestive Enzymes Activitymentioning
confidence: 99%
“…For trypsin and chymotrypsin, one unit of enzyme activity (U) was defined as the amount of enzyme that released 1 µmol of p-nitroanilide per min, using 8800 M cm −1 as the extinction coefficient, measured at 405 nm. The amylase activity was determined according to the Somogyi-Nelson method using soluble starch (2% w/v) as the substrate, as described by Robyt and Whelan [33]. One unit of activity (U) was defined as the amount of enzyme capable of producing 1 mg of maltose per minute.…”
Section: Digestive Enzymes Activitymentioning
confidence: 99%
“…The acid-stable a-amylase of Aspergillus niger produces mostly G^, slightly less G^, slightly less G^^ than G^, and very small quantities of G^ and G^ as final products on starch (Minoda e_t a%., 1968). The main end products of the hydrolysis of amylose produced by human salivary amylase are G^ and G^ with small quantities of and Gj^; the same is the case for porcine pancreatic amylase except that larger quantities of and G^ are produced (Robyt, 1962) . However, porcine pancreatic amylase has a degree of multiple attack of about six which is twice that of human salivary amylase (Sobyt and French,19Ô7).…”
Section: Discussionmentioning
confidence: 86%
“…The acid-stable a-amylase of Aspergillus niger produces mostly G^, slightly less G^, slightly less G^^ than G^, and very small quantities of G^ and G^ as final products on starch (Minoda e_t a%., 1968). The main end products of the hydrolysis of amylose produced by human salivary amylase are G^ and G^ with small quantities of and Gj^; the same is the case for porcine pancreatic amylase except that larger quantities of and G^ are produced (Robyt, 1962 Another advantage of using S. bovis for commercial amylase production would be that it is devoid of proteolytic activity (Deibel, 1964- (Prescott ^ al., 1959) or bicarbonate, and glutamine also serves as a sole source of nitrogen (Wolin 5^ et al, 1959). Wolin and Weinberg (I960) found that growth with ammonium salts, but not with glutamine, requires an un known substance formed by autoclaving phosphate with glucose.…”
Section: Discussionmentioning
confidence: 99%