Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 115, Issue -, Pages 1088-1093Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.04.154
Keywords
Pectinase immobilization; Thermodynamic parameters; Calcium alginate beads
Funding
- FACEPE (Foundation for Science and Technology of the State of Pernambuco, Brazil) [IBPG-0141-5.07/16]
- CNPq (National Council for Scientific and Technological Development, Brazil) [471773/2013-1]
- CAPES (National Council for the Improvement of Higher Education, Brazil) [23038.003634/2013-15]
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The kinetics and thermodynamics of Aspergillus aculeatus pectinase, either free or immobilized in alginate beads, were investigated. Pectinase immobilization ensured an enzyme immobilization yield of 59.71%. The irreversible denaturation of pectinase in both preparations was evaluated at temperatures ranging from 30 to 60 degrees C. When temperature was raised, the first-order thermal denaturation constant increased from 0.0011 to 0.0231 min(-1) for the free enzyme and from 0.0017 to 0.0700 min(-1) for the immobilized one, respectively. The results of residual activity tests enabled us to estimate, for denaturation of both free and immobilized pectinase, the activation energy (E*(d) = 85.1 and 101.6 kJ.mol(-1)), enthalpy (82.59 <= Delta H*(d) <= 82.34 kJ.mol(-1) and 99.11 5 <= Delta H*(d) <= 98.86 kJ.mol(-1)), entropy (-63.26 <= Delta S*(d) <= -63.85 J.mol(-l).K-1 and -5.50 <= Delta S-d(*) <= -5.23 J.mol(-l).K-1) and Gibbs free energy (101.8 <= Delta G*(d) <= 104.7 KJ.mol(-1) and 100.6 <= Delta G*(d) <= 102.0 k.mol(-1)). The integral activity of a continuous system using the free and immobilized enzyme was also predicted, whose results indicated a satisfactory enzyme long-term thermostability in both preparations at temperatures commonly used to clarify juice. These results suggest that both free and immobilized pectinase from A. aculeatus may be profitably exploited in future food industrial applications, with special concern to the immobilized enzyme because of its reusability. (C) 2018 Elsevier B.V. All rights reserved.
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