Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: The effect of high pressure homogenization on the activity of a commercial beta-galactosidase
Author: Tribst, AAL
Augusto, PED
Cristianini, M
Abstract: High pressure homogenization (HPH) has been proposed as a promising method for changing the activity and stability of enzymes. Therefore, this research studied the activity of beta-galactosidase before and after HPH. The enzyme solution at pH values of 6.4, 7.0, and 8.0 was processed at pressures of up to 150 MPa, and the effects of HPH were determined from the residual enzyme activity measured at 5, 30, and 45 A degrees C immediately after homogenization and after 1 day of refrigerated storage. The results indicated that at neutral pH the enzyme remained active at 30 A degrees C (optimum temperature) even after homogenization at pressures of up to 150 MPa. On the contrary, when the beta-galactosidase was homogenized at pH 6.4 and 8.0, a gradual loss of activity was observed, reaching a minimum activity (around 30 %) after HPH at 150 MPa and pH 8.0. After storage, only beta-galactosidase that underwent HPH at pH 7.0 retained similar activity to the native sample. Thus, HPH did not affect the activity and stability of beta-galactosidase only when the process was carried out at neutral pH; for the other conditions, HPH resulted in partial inactivation of the enzyme. Considering the use of beta-galactosidase to produce low lactose milk, it was concluded that HPH can be applied with no deleterious effects on enzyme activity.
Subject: Ultra high pressure homogenization
Enzyme activity
Non thermal technology
Low lactose milk
Country: Alemanha
Editor: Springer Heidelberg
Citation: Journal Of Industrial Microbiology & Biotechnology. Springer Heidelberg, v. 39, n. 11, n. 1587, n. 1596, 2012.
Rights: fechado
Identifier DOI: 10.1007/s10295-012-1179-9
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000310232200003.pdf741.01 kBAdobe PDFView/Open

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