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Characterization of Honey Amylase
Author(s) -
Babacan Sibel,
Rand Arthur G.
Publication year - 2007
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2006.00215.x
Subject(s) - amylase , starch , enzyme , chemistry , thermal stability , kinetics , food science , biochemistry , chromatography , nuclear chemistry , organic chemistry , physics , quantum mechanics
The major α‐amylase in honey was characterized. The optimum pH range and temperature were determined for the enzyme as 4.6 to 5.3 and 55 °C, respectively. The enzyme was stable at pH values from 7 to 8. The half‐lives of the purified enzyme at different temperatures were determined. The activation energy for heat inactivation of honey amylase was 114.6 kJ/mol. The enzyme exhibited Michaelis–Menten kinetics with soluble starch and gave K M and V max values of 0.72 mg/mL and 0.018 units/mL, respectively. The enzyme was inhibited by CuCl (34.3%), MgCl 2 (22.4%), and HgCl 2 (13.4%), while CaCl 2 , MnCl 2 , and ZnSO 4 did not have any effect. Starch had a protective effect on thermal stability of honey amylase. Therefore, it might be critical to process or control the amylase in honey before incorporation into starch‐containing foods to aid in the preservation of starch functionality. One step could involve heat treating honey with other ingredients, especially those that dilute and acidify the honey environment.