| Literature DB >> 11992533 |
B Ly Nguyen1, A Van Loey, D Fachin, I Verlent, M Hendrickx, I M Hendrickx.
Abstract
Pectin methylesterase (PME) was extracted from bananas (cv Cavendish) and purified by affinity chromatography on a CNBr-Sepharose-PME inhibitor (PMEI) column. A single protein and PME activity peak was obtained. For banana PME, a biochemical characterization in terms of molar mass (MM), pI, and kinetic parameters was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal inactivation of purified banana PME could be described by a first-order kinetic model in a temperature range of 65 degrees to 72.5 degrees C, whereas its isobaric-isothermal inactivation followed a fractional-conversion model. Banana PME was found to be more thermally stable compared with PMEs extracted from orange, tomato, and apple. Copyright 2002 Wiley Periodicals, Inc.Entities:
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Year: 2002 PMID: 11992533 DOI: 10.1002/bit.10249
Source DB: PubMed Journal: Biotechnol Bioeng ISSN: 0006-3592 Impact factor: 4.530