Technical note: A simplified procedure for myofibril hydrophobicity determination

Chelh, Ilham; Gatellier, Philippe; Santé-Lhoutellier, Véronique

doi:10.1016/j.meatsci.2006.05.019

Cited by 471 publications

(201 citation statements)

References 21 publications

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“…Hydrophobicity of myofibrillar protein was determined using the hydrophobic chromophore bromophenol blue (BPB) according to the method of Chelh et al [15]. e amount of bound BPB was expressed as the difference between total and free BPB and used as an index of hydrophobicity:…”

Section: Hydrophobicity Analysismentioning

confidence: 99%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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e e ects of freezing temperature on the microstructure and moisture migration of beef were investigated, aiming to provide the potential theoretical basis for the beef storage. Drip loss, surface hydrophobicity, and secondary structure of myo brillar proteins, ice crystal, and micro-and ultrastructure of meat were analyzed at 4°C, −1°C, −6°C, −9°C, −12°C, and −18°C, respectively. Results indicated that the drip loss and surface hydrophobicity of samples stored at −12°C were signi cantly lower than that stored at 4°C and −1°C (p < 0.05) and no signi cant di erence with −18°C (p > 0.05). Result from Fourier transform infrared spectroscopy suggested that protein denaturation occurred after storage. ere was an increase in α-helices and decline in random coil at lower temperature (−12°C and −18°C). It was indicated that the samples stored at −12°C and −18°C could e ectively restrain the denaturation of protein and maintain the stability of secondary structure. e analysis of the ice crystal and micro-and ultrastructure of the muscle indicated that the structure of samples stored at −12°C and −18°C had more integrity and was complete than that stored at 4°C and −1°C. e spaces (water "reservoir" and "channel") where was the origination of drip were small. Furthermore, the results of low-eld nuclear magnetic resonance and 1 H magnetic relaxation image showed that the freezing at −12°C could inhibit the migration of immobilized water to free water.

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Section: Hydrophobicity Analysismentioning

confidence: 99%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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“…Protein surface hydrophobicity of MP was determined using bromophenol blue (BPB) as detailed by Chelh, Gatellier, and Sante-Lhoutellier [16]. The absorbance of the supernatant was measured at 595 nm against the reagent blank.…”

Section: Protein Surface Hydrophobicitymentioning

confidence: 99%

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

et al. 2016

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Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.

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“…The hydrophobic ability of myofibril proteins was determined by the method of Chelh et al (2006) with minor changes. Forty microliter of 1 mg/mL bromophenol blue (BPB) was added to 2 mL myofibril suspension (2 mg/mL).…”

Section: Determination Of Protein Surface Hydrophobicitymentioning

confidence: 99%

Effects of High Oxygen Packaging on Tenderness and Water Holding Capacity of Pork Through Protein Oxidation

Lin

Zhou

Zhang

2015

Food Bioprocess Technol

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The objective of this study was to investigate the biochemical difference of pork under high oxygen modified atmosphere packaging and their contribution to meat tenderness and water holding capacity of pork during postmortem storage. Twelve longissimus dorsi muscles were randomly assigned to either high oxygen modified atmosphere packaging or vacuum packaging and stored for 1, 4, and 6 days at 4°C. The carbonyl content, protein surface hydrophobicity, protein solubility, calpain activity, desmin degradation, tenderness, and water loss of pork were determined. Results showed that carbonyl content, protein surface hydrophobicity, and protein solubility were significantly affected (P < 0.05) by packaging method, while storage time did not significantly influence protein surface hydrophobicity and the solubility of sarcoplasmic protein (P > 0.05). Samples from high oxygen modified atmosphere packaging at 1 day showed greater intensity of intact 80 KDa calpain and lower intensity of autolyzed 76 KDa calpain product compared to samples from vacuum packaging (P < 0.05). Desmin degradation was significantly affected (P < 0.05) by packaging method and storage time, while their interaction presented no significance (P > 0.05). Higher intensity of intact desmin was observed in samples from high oxygen modified atmosphere packaging than vacuum packaging samples from 1 day of postmortem storage. Both packaging method and storage time showed significant effects (P < 0.05) on tenderness and water loss of pork muscle during postmortem storage. Changes in protein oxidation, calpain activation, and protein proteolysis of postmortem pork under high oxygen modified atmosphere packaging could help to explain decreased meat tenderness and increased centrifuge loss of pork. Keywords High oxygen modified atmosphere packaging . Pork muscle . Protein oxidation . Calpain . Tenderness . Water holding capacity Abbreviations HiOx High oxygen modified atmosphere packaging VP Vacuum packaging WHC Water holding capacity WBSF Warner-Bratzler shear force LD Longissimus dorsi PM Packaging method ST Storage time PM × ST Interaction of packaging method and storage time LF-NMR Low-field nuclear magnetic resonance DNPH 2,4-Dinitrophenylhydrazine BPB Bromophenol blue

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Technical note: A simplified procedure for myofibril hydrophobicity determination

Cited by 471 publications

References 21 publications

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

Effects of High Oxygen Packaging on Tenderness and Water Holding Capacity of Pork Through Protein Oxidation

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