Kinetic and thermodynamic study of aspartic protease extracted from Withania coagulans

被引：11
作者：
Ahmadi, Salman [1 ]
Salehi, Mahmoud [2 ]
Ausi, Solmaz [3 ]
机构：
[1] Univ Guilan, Fac Basic Sci, Dept Biol, Rasht, Iran
[2] Gonbad Kavous Univ, Fac Basic Sci & Engn, Dept Biol, Gonbad Kavous, Iran
[3] Gonbad Kavous Univ, Fac Basic Sci & Engn, Dept Chem, Gonbad Kavous, Iran
来源：
INTERNATIONAL DAIRY JOURNAL | 2021年 / 116卷
关键词：
THERMOSTABLE ENZYMES; THERMAL INACTIVATION; ACID PROTEASE; PURIFICATION; MILK; TEMPERATURE; PARAMETERS; STABILITY; XYLANASE; PH;
D O I：
10.1016/j.idairyj.2020.104960
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
The kinetic and thermodynamic parameters of the enzymatic reaction of aspartic protease extracted from Withania coagulans were investigated. The activation energy, Delta H-# , Delta S-# , and Delta G(# )of casein hydrolysis were 34.677 kJ mol(-1), 31.96-32.16 kJ mol(-1), -131.26 to -125.0 J mol(-1) , and 70.62-72.96 kJ mol(-1), respectively, which show the favourable formation of the enzyme-substrate complex, high tendency of the enzyme to casein hydrolysis and its spontaneous conversion to product. The half-life of the enzyme indicates its stability as a function of temperature. The calculated Z-value shows that D-value decreases ten times as a consequence of increasing the temperature by 8.6 degrees C. The activation energy (254.43 kJ mol(-1)), Delta H-# (251.54-251.71 kJ mol(-1)), Delta S-# (424.12-425.36 kJ mol(-1)) and Delta G(#) (103.52-112.6 kJ mol(-1)) for protease inactivation indicate high stability, compaction and enzyme resistance to thermal denaturation. Overall, these features make it a suitable industrial enzyme. (C) 2020 Elsevier Ltd. All rights reserved.
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页数：11
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共 51 条
[1]   Catalytic, kinetic and thermodynamic properties of stabilized Bacillus stearothermophilus alkaline protease [J].
Abdel-Naby, Mohamed A. ;
Ahmed, Samia A. ;
Wehaidy, Hala R. ;
El-Mandy, Said A. .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2017, 96 :265-271
[2]   Catalytic, kinetic and thermodynamic properties of Bacillus pumilus FH9 keratinase conjugated with activated pectin [J].
Abdel-Naby, Mohamed A. ;
Ibrahim, M. H. A. ;
El-Refai, H. A. .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2016, 85 :238-245
[3]   Characterisation of partially purified milk-clotting enzyme from Solanum dubium Fresen seeds [J].
Ahmed, Isam Ali Mohamed ;
Morishima, Isao ;
Babiker, Elfadil E. ;
Mori, Nobuhiro .
FOOD CHEMISTRY, 2009, 116 (02) :395-400
[4]   Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes [J].
Anthon, GE ;
Barrett, DM .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2002, 50 (14) :4119-4125
[5]   Effect of pH and temperature on stability and kinetics of novel extracellular serine alkaline protease (70 kDa) [J].
Bhunia, Biswanath ;
Basak, Bikram ;
Mandal, Tamal ;
Bhattacharya, Pinaki ;
Dey, Apurba .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2013, 54 :1-8
[6]   Proteases in organic synthesis [J].
Bordusa, F .
CHEMICAL REVIEWS, 2002, 102 (12) :4817-4867
[7]   The search for the ideal biocatalyst [J].
Burton, SG ;
Cowan, DA ;
Woodley, JM .
NATURE BIOTECHNOLOGY, 2002, 20 (01) :37-45
[8]   Thermodynamic investigation of an alkaline protease from Aspergillus tamarii URM4634: A comparative approach between crude extract and purified enzyme [J].
da Silva, Osmar Soares ;
de Oliveira, Rodrigo Lira ;
Silva, Jonatas de Carvalho ;
Converti, Attilio ;
Porto, Tatiana Souza .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2018, 109 :1039-1044
[9]   A new understanding of how temperature affects the catalytic activity of enzymes [J].
Daniel, Roy M. ;
Danson, Michael J. .
TRENDS IN BIOCHEMICAL SCIENCES, 2010, 35 (10) :584-591
[10]   Thermodynamic and kinetic studies on pectinase extracted from Aspergillus aculeatus: Free and immobilized enzyme entrapped in alginate beads [J].
de Oliveira, Rodrigo Lira ;
da Silva, Osmar Soares ;
Converti, Attilio ;
Porto, Tatiana Souza .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2018, 115 :1088-1093
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