Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/75082
Type: Artigo de periódico
Title: The effect of the high pressure homogenisation on the activity and stability of a commercial neutral protease from Bacillus subtilis
Author: Tribst, AAL
Augusto, PED
Cristianini, M
Abstract: The activity of a commercial neutral protease from Bacillus subtilis after high pressure homogenisation (HPH) was investigated. The enzyme was processed up to 2000 bar, and the residual activity was measured from 20 to 70 degrees C during refrigerated storage. Moreover, the effect of HPH at high temperatures was evaluated. No improvement in the activities at 5570 degrees C were observed after HPH, while an increase of approximately 30% in the 20 degrees C-activity was reached after 2000 bar processing. Thus, HPH shifted the optimum temperature from 55 to 20 degrees C. The high temperature homogenisation caused no changes in 55 degrees C-activity, but reduced 20 degrees C-activity three times. It suggests that HPH modifies the protease configuration, changing enzyme performance (maximum activity condition), as the efficacy of lock-and-key mechanism is strictly dependent on enzyme spatial structure. The changes can be permanent or not, depending on homogenisation pressure, inlet temperature and enzyme storage conditions. Therefore, the HPH is a promising method to change protease characteristics.
Subject: Enzymatic activity
high pressure homogenisation
protease
Country: EUA
Editor: Wiley-blackwell
Rights: fechado
Identifier DOI: 10.1111/j.1365-2621.2011.02898.x
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000301717300008.pdf886.89 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.