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Original Article



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

Arumugam Vengadaramana, Mehala Uthayasooriyan, Thananthika Sittampalam, Nirosha Razeek, Ranganathan Kapilan.




Abstract
Cited by 3 Articles

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.

Key words: Amylase, enzyme activity, enzyme stability, starch, zero order kinetics






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