Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/241655
Type: Artigo de periódico
Title: Comparative Effects Of High Isostatic Pressure And Thermal Processing On The Inactivation Of Rhizomucor Miehei Protease
Author: de Castro Leite Junior
Bruno Ricardo; Lima Tribst
Alline Artigiani; Cristianini
Marcelo
Abstract: This study compared the inactivation of the proteolytic (PA) and milk-clotting (MCA) activities of Rhizomucor miehei protease by high isostatic pressure (HIP) up to 600 MPa/20 min/25 degrees C and by a thermal process (TP) up to 72.0 degrees C/30 min. Pressures above 300 MPa caused a loss of enzyme activity, MCA being expressively more affected than PA. The inactivation of the protease showed a nonlinear behavior, converging to a two-component system model (stable and labile fractions). The stable fraction represents higher activity for PA and the labile for MCA. The D-values for stable PA (3.35 +/- 0.42 min for HIP and 5.58 +/- 0.48 min for TP) and labile MCA (0.34 +/- 0.04 min for HIP and 0.47 +/- 0.04 min for TP) were significantly lower for the HIP processed enzyme, highlighting the effectiveness of the process in inactivating this enzyme. Therefore, the results highlight HIP at 600 MPa as an optional process to inactivate R. miehei protease (without the use of heat), being more effective than the thermal process. (C) 2015 Elsevier Ltd. All rights reserved.
Subject: Milk-clotting Activities
Enzymes
Homogenization
Chymosin
Country: AMSTERDAM
Editor: ELSEVIER SCIENCE BV
Citation: Comparative Effects Of High Isostatic Pressure And Thermal Processing On The Inactivation Of Rhizomucor Miehei Protease. Elsevier Science Bv, v. 65, p. 1050-1053 JAN-2016.
Rights: embargo
Identifier DOI: 10.1016/j.lwt.2015.09.042
Address: http://www.sciencedirect.com/science/article/pii/S0023643815302140
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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