Immobilization of β-galactosidase by complexation: Effect of interaction on the properties of the enzyme.

Autor:	Souza CJF; Universidade de São Paulo, Faculdade de Zootecnia e Engenharia de Alimentos, Av. Duque de Caxias Norte, 225, CP 23, CEP 13535 900 Pirassununga, São Paulo, Brazil; Universidade Federal da Grande Dourados, Faculdade de Engenharia, Pós-graduação em Ciência e Tecnologia de Alimentos, PO Box 533, 79804-970 Dourados, Brazil., Garcia-Rojas EE; Laboratório de Engenharia e Tecnologia Agroindustrial (LETA), Universidade Federal Fluminense (UFF), Av. dos Trabalhadores, 420, Volta Redonda, RJ 27255-125, Brazil., Souza CSF; Laboratório de Engenharia e Tecnologia Agroindustrial (LETA), Universidade Federal Fluminense (UFF), Av. dos Trabalhadores, 420, Volta Redonda, RJ 27255-125, Brazil., Vriesmann LC; Universidade Federal do Paraná, Departamento de Bioquímica e Biologia Molecular, CP 19046, 81531-980 Curitiba, PR, Brazil., Vicente J; Programa de Pós-graduação em Ciência e Tecnologia de Alimentos (PPGCTA), Universidade Federal Rural do Rio de Janeiro (UFRRJ), Rodovia BR 465, Km 7, Seropédica, RJ 23890-000, Brazil., de Carvalho MG; Programa de Pós-Graduação em Química (PPGQ), Departamento de Química-ICE, Universidade Federal Rural do Rio de Janeiro (UFRRJ), Rodovia BR 465, Km 7, Seropédica, RJ 23890-000, Brazil., Petkowicz CLO; Universidade Federal do Paraná, Departamento de Bioquímica e Biologia Molecular, CP 19046, 81531-980 Curitiba, PR, Brazil., Favaro-Trindade CS; Universidade de São Paulo, Faculdade de Zootecnia e Engenharia de Alimentos, Av. Duque de Caxias Norte, 225, CP 23, CEP 13535 900 Pirassununga, São Paulo, Brazil. Electronic address: carmenft@usp.br.
Jazyk:	angličtina
Zdroj:	International journal of biological macromolecules [Int J Biol Macromol] 2019 Feb 01; Vol. 122, pp. 594-602. Date of Electronic Publication: 2018 Nov 04.
DOI:	10.1016/j.ijbiomac.2018.11.007
Abstrakt:	In the present work, we aimed to explore the molecular binding between alginate and β-galactosidase, as well as the effect of this interaction on the activity retention, thermal stability, and kinetic properties of the enzyme. The impact of pH and enzyme/alginate ratio on physicochemical properties (turbidity, morphology, particle size distribution, ζ-potential, FTIR, and isothermal titration calorimetry) was also evaluated. The ratio of biopolymers and pH of the system directly affected the critical pH of complex formation; however, a low alginate concentration (0.1 wt%) could achieve an electrical charge equivalence at pH 3.4 with 93.72% of yield. The binding between β-galactosidase and alginate was an equilibrium between enthalpic and entropic contributions, which promoted changes in the structure of the enzyme. Nevertheless, this conformational modification was reversible after the dissociation of the complex, which allowed the enzyme to regain its activity. These findings will likely broaden functional applications of enzyme immobilization. (Copyright © 2018. Published by Elsevier B.V.)
Databáze:	MEDLINE
Externí odkaz:	Full Text from ScienceDirect