1998
DOI: 10.1590/s1516-89131998000100003
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Determination of amylase activity in cotyledons of Phaseolus vulgaris L. cv. carioca

Abstract: Determination of α- and β-amylase activity in the extracts of cotyledons of Phaseolus vulgaris L. cv. cariocawas done using selective inactivation of α-amylase by lowering the pH of the incubation medium or by the use of EDTA as inhibitor or selective inactivation of β-amylase by the use of HgCl2 or by heating to 70ºC in the presence of CaCl2; and still by using the reagent starch azure for specific determination of α-amylase. Results indicated that the methods used were inappropriate … Show more

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Cited by 7 publications
(4 citation statements)
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“…Unless there is a specific substrate to measure α- or β-amylase activity, it is necessary to inactivate one of the enzymes, especially in crude extracts. The commonly used procedures are based on selective inactivation of α-amylase by EDTA ( , ) or inactivation of β-amylase by thermal treatment or HgCl 2 ( , ). The specificity of the thermal treatment is questionable, because there are heat labile α-amylases from some plant species which could be inactivated by heat ( , ).…”
Section: Resultsmentioning
confidence: 99%
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“…Unless there is a specific substrate to measure α- or β-amylase activity, it is necessary to inactivate one of the enzymes, especially in crude extracts. The commonly used procedures are based on selective inactivation of α-amylase by EDTA ( , ) or inactivation of β-amylase by thermal treatment or HgCl 2 ( , ). The specificity of the thermal treatment is questionable, because there are heat labile α-amylases from some plant species which could be inactivated by heat ( , ).…”
Section: Resultsmentioning
confidence: 99%
“…EDTA has been largely used as an α-amylase inhibitor by chelating the calcium present in the enzyme molecules altering their stability ( , ), and HgCl 2 treatments have been used for β-amylase inactivation, but there are controversies about the specificity and efficiency of these inhibitors ( , ).…”
Section: Resultsmentioning
confidence: 99%
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“…Thirteen milliliters of distilled water were added to the samples, and absorbance changes were recorded at 620 nm. One unit of amylase activity was identified as the quantity of enzyme that caused the changes in the absorbance of 0.1 [ 35 ].…”
Section: Methodsmentioning
confidence: 99%