Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/352216
Type: Artigo
Title: Biophysical evaluation of milk-clotting enzymes processed by high pressure
Author: Leite Júnior, Bruno Ricardo de Castro
Tribst, Alline Artigiani Lima
Grant, Nicholas J.
Yada, Rickey Y.
Cristianini, Marcelo
Abstract: High pressure processing (HPP) is able to promote changes in enzymes structure. This study evaluated the effect of HP on the structural changes in milk-clotting enzymes processed under activation conditions for recombinant camel chymosin (212 MPa/5 min/10 °C), calf rennet (280 MPa/20 min/25 °C), bovine rennet (222 MPa/5 min/23 °C), and porcine pepsin (50 MPa/5 min/20 °C) and under inactivation conditions for all enzymes (600 MPa/10 min/25 °C) including the protease from Rhizomucor miehei. In general, it was found that the HPP at activation conditions was able to increase the intrinsic fluorescence of samples with high pepsin concentration (porcine pepsin and bovine rennet), increase significantly the surface hydrophobicity and induce changes in secondary structure of all enzymes. Under inactivation conditions, increases in surface hydrophobicity and a reduction of intrinsic fluorescence were observed, suggesting a higher exposure of hydrophobic sites followed by water quenching of Trp residues. Moreover, changes in secondary structure were observed (with minor changes seen in Rhizomucor miehei protease). In conclusion, HPP was able to unfold milk-clotting enzymes even under activation conditions, and the porcine pepsin and bovine rennet were more sensitive to HPP
Subject: Enzimas
Country: Reino Unido
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.foodres.2017.03.042
Address: https://www.sciencedirect.com/science/article/pii/S0963996917301424
Date Issue: 2017
Appears in Collections:FEA - Artigos e Outros Documentos
NEPA - Artigos e Outros Documentos

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