Food Chemistry

2.5 Kinetics of Enzyme-Catalyzed Reactions 117 the first product, glyceraldehyde-3-phosphate, is released. An enamine rearrangem ...

118 2 Enzymes termediary enzyme-substrate complex, EA. The complex then forms the product P and releases the free enzyme: (2.30) ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 119 Under steady-state conditions the rates of break- down and formation of EA are eq ...

120 2 Enzymes Table 2.9.Rate constants for some enzyme catalyzed reactions Enzyme Substrate k 1 K− 1 k 0 (l·mol−^1 s−^1 )(s−^1 ) ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 121 Fig. 2.23.Determination of Kmand V (according to LineweaverandBurk) υ 0 =−Km υ 0 ...

122 2 Enzymes mechanism: (2.51) In an “ordered mechanism” the binding during the catalyzed reaction according to equation 2.49 i ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 123 substrate reaction is expressed in the following form: υ 0 = V 1 + Ka (A 0 ) (2.5 ...

124 2 Enzymes Fig. 2.26.Plotting slopes (a) and ordinate intercepts (b) from Fig. 2.25 versus 1/[A 0 ] Fig. 2.27.Evaluation of a ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 125 indicative of positive cooperation. Each substrate molecule, often called an effe ...

126 2 Enzymes and concentration of inhibitors, i. e. compounds which decrease the rate of catalysis, and activa- tors, which hav ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 127 Table 2.10.Examples of reversible enzyme inhibition Enzyme EC- Sustrate Inhibitor ...

128 2 Enzymes bitor; Km is unchanged whereas the values of V are decreased such that V becomes V/( 1 +[I]/Ki), i. e. non-competi ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 129 Table 2.11.pH Optima of various enzymes Enzyme Source Substrate pH Optimum Pepsin ...

130 2 Enzymes In order to better understand the form of the enzyme involved in catalysis, a hypothetical enzyme-substrate system ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 131 Table 2.12.Thermal inactivation of enzymes to prevent deterioration of food quali ...

132 2 Enzymes For the reaction rate follows: k=M· A A^ = =M· k 1 k− 1 =M·K^ = (2.86) with M= KB·T h = R·T NA·h (2.87) (K#equilib ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 133 and lnt=+ Ea RT +const. (2.100) When plotting lnt against 1/T, a family of par- a ...

134 2 Enzymes Fig. 2.35.Fungalα-amylase. Amylose hydrolysis ver- sus temperature.Arrheniusdiagram for assessing the activation e ...

2.5 Kinetics of Enzyme-Catalyzed Reactions 135 Fig. 2.37.Thermal inactivation of enzymes of milk. 1 Lipase (inactivation extent, ...

136 2 Enzymes Fig. 2.40.Blanching of semiripened peas at 95◦C; lipoxygenase inactivation (according to Svensson, 1977).Experime ...