Research Article | Volume: 4, Issue: 3, May-June, 2016

The Characterization of Amylolytic Enzyme Present in Fermented Sweet Sap of Palmyrah

Arumugam Vengadaramana Mehala Uthayasooriyan Thananthika Sittampalam Nirosha Razeek Ranganathan Kapilan   

Open Access   

Published:  Jun 21, 2016

DOI: 10.7324/JABB.2016.40304

Amylase enzyme obtained from 12h of naturally fermented sweet sap of palmyrah. The amylase showed zero order kinetics for 10min. The optimum temperature for the activities of enzyme as 65oC and pH was 7.0. When the enzyme was pre-incubated at 65oC and at pH 7.0, it lost 62% of its initial activity at 60min. This enzyme showed activity with starch, lactose, maltose, pectin and sucrose. Amylase activity was strongly inhibited by 2mM of Hg2+ but 2 mM of Ca2+, Ba2+, Mg2+, Mn2+, Na+, Zn2+, Mn2+ and Cu2+ stimulated the enzyme activity at 65 oC and at pH 7.0. The enzyme in the presence of 2mM Mn2+, Cu2+ and Na+ separately, retained 79, 86 and 68 % of its initial activity respectively at 60 min, 65oC and pH 7.0.

Keyword:     Amylaseenzyme activityenzyme stabilitystarchzero order kinetics.


Vengadaramana A, Uthayasooriyan M, Sittampalam T, Razeek N, Kapilan R. The Characterization of Amylolytic Enzyme Present in Fermented Sweet Sap of Palmyrah. J App Biol Biotech. 2016; 4 (03): 020-023. DOI: 10.7324/JABB.2016.40304

Copyright: Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license.

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