Technical note: A simplified procedure for myofibril hydrophobicity determination |
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| Affiliation: | 1. State Key Laboratory of Food Science and Technology, Nanchang University, Jiangxi 330047, China;2. College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China;1. Hepatopancreatobiliary Surgery Department, the First Affiliated Hospital of Fujian Medical University, National Abdominal Surgery Institute of Fujian, Fuzhou City, Fujian, PR China;2. General Surgery Department, Luohe Central Hospital, Luohe, Henan, PR China;3. Department of Gynecology, Longyan First Hospital, Longyan, Fujian, PR China;1. Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark;2. The Niels Bohr Institute, Faculty of Science, University of Copenhagen, Universitetsparken 5, DK-2100 København Ø, Denmark;1. Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China;2. Food Science & Nutrition Department of Nanjing Normal University, Nanjing 210097, China |
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| 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. |
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