Thermal inactivation kinetics and thermodynamic properties of immobilised Aspergillus niger pectinase in rigid polyurethane foam

被引:0
|
作者
Bustamante-Vargas, C. E. [1 ]
Junges, A. [2 ]
Venquiaruto, L. D. [3 ]
Oro, C. E. D. [2 ]
Julio-Orozco, D. J. [4 ]
Zabot, G. L. [5 ]
Tres, M., V [5 ]
Paroul, N. [2 ]
Backes, G. T. [2 ]
Dallago, R. M. [2 ]
机构
[1] Univ Cordoba, Food Engn Dept, POB 230002, Cordoba, Colombia
[2] Univ Reg Alto Uruguai & Missoes, Dept Agr Sci, URI Erechim, POB 743, BR-99709910 Erechim, RS, Brazil
[3] Univ Reg Alto Uruguai & Missoes, Dept Exact & Earth Sci, URI Erechim, POB 743, BR-99709910 Erechim, RS, Brazil
[4] Univ Passo Fundo, Dept Engn, BR 285, BR-99052900 Passo Fundo, RS, Brazil
[5] Fed Univ Santa Maria UFSM, LAPE, Ctr DC, 1040 Sete Setembro St, BR-96508010 Cachoeira Do Sul, RS, Brazil
来源
INTERNATIONAL FOOD RESEARCH JOURNAL | 2019年 / 26卷 / 05期
关键词
Immobilised pectinase; Kinetic modelling; Thermal stability; Rigid foam polyurethane (RFPU); BETA-GALACTOSIDASE; PECTATE LYASE; POLYGALACTURONASE; BEHAVIOR; DEACTIVATION; HYDROLYSIS; PARAMETERS; STABILITY; PROTEASE; JUICE;
D O I
暂无
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The present work was performed in order to investigate the effect of in situ immobilisation of commercial Aspergillus niger pectinase in rigid polyurethane foam (RFPU) on thermal stability. Pectinase (liquid, lyophilised, and immobilised) was incubated from 50 to 80 degrees C. Residual activity data were fit to various kinetic models, which were rigorously evaluated by statistical and physical criteria. The first-order model provided the best fit to describe the thermal deactivation of pectinase. Immobilised pectinase exhibited higher thermal stability, presenting lower K-d-values (0.0015-0.0157 h(-1)) and higher half-life (t(1/2); 456.89-44.01 h), D (1517.86-146.22 h) and Z (29.85 degrees C) values. Thermodynamic parameters (Delta G*, Delta H* and Delta S*) corroborate that immobilised pectinase is thermodynamically more stable if compared to its free and non-immobilised forms (liquid and lyophilized), suggesting that their functionally active conformation was more conserved during the heat treatment. The feasibility of immobilisation is presented towards improving the thermal stability and the resistance to irreversible deactivation of pectinase. (C) All Rights Reserved
引用
收藏
页码:1535 / 1545
页数:11
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