A study of starch hydrolysis by α-amylase from porcine pancreas with deactivation of enzyme

被引：0

作者：

Milek, Justyna ^{[1
]}

Grubecki, Ireneusz ^{[2
]}

Tomczak, Wirginia ^{[2
]}

机构：

[1] Bydgoszcz Univ Sci & Technol, Fac Chem Technol & Engn, Dept Chem & Biochem Engn, Semianryjna 3, PL-85326 Bydgoszcz, Poland

[2] Cracow Univ Technol, Fac Chem Engn & Technol, Warszawska 24, PL-31155 Krakow, Poland

来源：

CHEMICAL AND PROCESS ENGINEERING-NEW FRONTIERS | 2024年 / 45卷 / 02期

关键词：

alpha-amylase from porcine pancreas; starch hydrolysis; activation energy; deactivation energy; ACTIVATION-ENERGIES; INACTIVATION; IMMOBILIZATION; PURIFICATION; TEMPERATURE; STABILITY; MODEL;

D O I：

10.24425/cpe.2024.148551

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

The demand for energy and the search for alternative energy sources are the reasons why scientists are interested in starch hydrolysis. The aim of this work was to experimentally study the hydrolysis of starch by alpha-amylase from porcine pancreas with a-amylase deactivation. Based on the experimental data, the parameters of starch hydrolysis by alpha-amylase with deactivation of enzyme were estimated. A mathematical model of temperature impact on the activity of alpha-amylase from porcine pancreas was used. It was estimated that the activation energy E-a and the deactivation energy E(d )were equal to 66 +/- 4 kJ/mol and 161 +/- 12 kJ/mol, respectively. Additionally, specific constant of starch hydrolysis k(0) and specific constant of a-amylase deactivation k(d0) were calculated. The optimum temperature T-opt equal to 318 +/- 0:5 K was obtained from the mathematical model. The obtained values of E-a, E-d; k(0 ) and k(d0 )parameters were used to conduct the model starch hydrolysis by alpha-amylase from porcine pancreas at 310 K and 333 K.

引用

页数：8

共 38 条

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