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Study of Activation and Inhibition of Certain Metal Ions to Amylase Catalyzed Reaction by Microcalorimetry
Author(s) -
Zhang HongLin,
Yu XhiFang,
Nie Yi,
Liu XiaoJing,
Zhang Gang
Publication year - 2003
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20030211114
Subject(s) - chemistry , michaelis–menten kinetics , activator (genetics) , isothermal microcalorimetry , catalysis , metal , amylase , metal ions in aqueous solution , nuclear chemistry , ion , enzyme , enzyme assay , biochemistry , thermodynamics , organic chemistry , enthalpy , physics , gene
With or without activation or inhibition of metal ion, the power‐time curves of amylase catalyzed reaction were determined by a 2277 thermal activity monitor (Sweden). The Michaelis constant ( K ), apparent Michaelis constant ( K m ), maximum velocity ( v m ) and apparent maximum velocity ( v am ) of amylase catalyzed reaction were obtained using thermokinetic theory and reduced extent method. On the basis of data obtained, the following relationships between K m and concentration of metal ion ( c ) were established for inhibitor of Ni 2+ K m = 2.9648 × 10 −3 ‐1.3912 × 10 −4 c R =0.9998 for inhibitor of Co 2+ K m = 1.0227 × 10 −3 + 8.2676 × 10 −6 c R = 0.9955 for activator of Ca 2+ K m = 1.0630 × 10– 7 c 2‐ 1.8311 × 10 −6 c + 9.3058 × 10 −6 R = 0.9999 for activator of Li + K m = 5.6300 × 10– 8 c 2‐ 1.5329 × 10 −6 c + 1.2662 × 10 −5 R = 0.9999 The K m ‐ c relationships show a strenuous inhibitory effect for Ni 2+ and a strenuous active effect for Ca 2+ .