| Literature DB >> 22063223 |
Ilham Chelh1, Philippe Gatellier, Véronique Santé-Lhoutellier.
Abstract
A simple and reliable method for the determination of surface hydrophobicity of nonsolubilized myofibrils (from pig M. longissimus dorsi) was developed and validated. This method is based on the interaction of the hydrophobic chromophore bromophenol blue (BPB) with myofibrillar proteins and the separation of free and bound BPB by centrifugation. The titration of bound BPB is performed by absorption spectroscopy, and the amount of bound BPB is considered as an index of protein hydrophobicity. Heating, which is known to increase protein hydrophobicity, was performed in order to validate this method. Fixation of BPB to myofibrils increased with heating time and temperature, strongly suggesting that it may be closely related to protein hydrophobicity.Entities:
Year: 2006 PMID： 22063223 DOI： 10.1016/j.meatsci.2006.05.019
Source DB: PubMed Journal: Meat Sci ISSN： 0309-1740 Impact factor: 5.209