Heat-induced changes in sulfhydryl groups of harp seal muscle proteins

Synowiecki, J.; Shahidi, Fereidoon

doi:10.1021/jf00011a026

Cited by 21 publications

(19 citation statements)

References 13 publications

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“…However, the data from the present study contrast with the findings of Synowiecki and Shahidi (1991), who reported a decrease in the content of sulfhydryl groups and an increase in the content of disulfide bonds on heating seal meat proteins. Together, these results would suggest that the process of sulfhydryl-disulfide changes occurring in seal meat proteins, as described by Synowiecki and Shahidi (1991), may be essentially one of disulfide cross-linking of protein molecules due to oxidation of sulfhydryl to disulfide groups, while the extrusion of wheat proteins, as reported in the present study, appeared to result in the reduction of disulfide groups to sulfhydryls. Secondly, the involvement of shear force in extrusion, as in the present study, as opposed to ordinary heating alone, may be a significant factor in the differences between the results.…”

Section: Disulfide and Sulfhydryl Analysiscontrasting

confidence: 99%

“…Sulfhydryl groups and disulfide bonds also contribute to the stability of the native conformations of proteins and are thus important in maintaining structure and functional properties of native proteins (Thannhauser et al 1987, Synowiecki andShahidi 1991), as well as the texture of cereal-based products (Chan and Wasserman 1993). Several studies have attempted to relate the disulfide and sulfhydryl contents of extrudates to some properties of the extrudates.…”

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Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Anderson¹,

2000

Cereal Chem

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Cereal Chem. 77(3):354-359Twin-screw extrusion of wheat flour and the effects on the flour proteins were studied using flour samples containing 9, 20, and 30% protein. Vital gluten containing 70% protein was used to achieve the flour protein levels. The three flour samples were extruded with a twin-screw extruder at a combination of processing parameters (exit die temperatures of 120, 140, and 160°C, and screw speeds of 240, 320, and 400 rpm). Increasing extruder exit die temperatures resulted in increased sulfhydryl content of the 9 and 20% protein content flour samples, but appeared to have little or no effect on the 30% protein content flour sample. Similarly, disulfide content decreased, albeit disproportionately, following the same trend. Both sulfhydryl and disulfide contents of extruded samples were lower than those of the nonextruded samples and could imply denaturation of protein, aggregation through intermolecular disulfide bonds, or oxidation during extrusion processing. Total cysteine content of extruded samples decreased by ≈16% relative to nonextruded samples, but otherwise remained almost unchanged among all extruded samples. The loss of total cysteine in extruded samples could represent the generation of hydrogen sulfide, volatile organic compounds, or flavor compounds during extrusion. SDS-PAGE analysis of total proteins showed a shift from the higher to lower molecular weight regions for certain protein bands. Both depolymerization and protein aggregation occurred at higher shear forces during extrusion.

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Section: Disulfide and Sulfhydryl Analysiscontrasting

confidence: 99%

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confidence: 99%

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Anderson¹,

2000

Cereal Chem

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“…Disulfide bonds were reduced to sulfhydryl groups using sodium borohydride. Determination of sulfhydryl groups before and after reduction was carried out using DTNB, according to the method described by Synowiecki and Shahidi (1991).…”

Section: Determination Of Sulfhydryl Groups and Disulfide Bondsmentioning

confidence: 99%

Gelation of Proteins from Washed Muscle of Threadfin Bream (Nemipterus japonicus) under Mild Acidic Conditions

Chawla

Venugopal

Nair

1996

Journal of Food Science

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Gelation of proteins of washed mince of threadfin bream was induced by the organic acids: acetic, lactic, tartaric, and citric. Washing of mince was essential for gelation. The strength of acetic acid-induced gel was affected by setting conditions and heat treatment. Gelation was associated with degradation of myosin heavy chain and appearance of a new protein band of about 160 kDa. Solubility studies of the gel in various solvents suggested structural changes. Gelation was also associated with oxidation of sulfhydryl groups. Salts negatively influenced gelation.

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“…In both these processes fish protein is subjected to heating and dehydration, though the actual conditions of processing vary widely. While the biochemical and nutritional changes occurring in fish muscle proteins during heating at high temperature (100°C and higher) have been extensively studied (Bjarnarson and Carpenter 1970 Synowiecki and Shahidi 1991). Whether the course of such changes in proteins is altered by the additional influence of dehydration is not fully known.…”

Section: Introductionmentioning

confidence: 99%

Biochemical and nutritional changes in fish proteins during drying

et al. 1995

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Biochemical and nutritional changes in the muscle proteins of a lean marine fish Nempiterus japonicus during drying at 50, 60 and 70°C were investigated. Solubility of proteins in water, 0.6 M NaCI, 1.5 M urea, 8 M urea and 10 g litre-* sodium dodecyl sulphate (SDS) decreased as drying progressed at all three temperatures; most of the decrease occurring in the initial 4 h of drying. SDS-polyacrylamide gel electrophoresis of 1.5 M urea, 8 M urea and SDS extracts showed that higher molecular weight (MW) protein fractions were more sensitive to drying and disappeared much earlier from electropherograms than the lower MW protein fractions. Residual solubility of proteins near the pH range of 4-6 was found to increase during drying, but solubility at acid and alkaline pH was adversely affected. Decrease of solubility by drying was more affected at acid pH, especially at higher temperatures than at alkaline pH. Sulphydryl groups registered a regular and sharp decrease with drying except at 5WC, where initially an increase was observed. Apart from disulphide and hydrophobic bonds, free amino groups also appear to be involved in denaturation reactions during drying. Pepsin digestibility of fish muscle decreased slightly during drying but a clear relationship with drying temperature was not evident. Highly significant differences in proteins between protein efficiency ratio (PER), net protein utilisation (NPU) and biological value were observed between the drying temperatures. The PER and NPU of fish dried at 60°C were significantly higher than those dried at 50 or 70°C.

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Heat-induced changes in sulfhydryl groups of harp seal muscle proteins

Cited by 21 publications

References 13 publications

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Gelation of Proteins from Washed Muscle of Threadfin Bream (Nemipterus japonicus) under Mild Acidic Conditions

Biochemical and nutritional changes in fish proteins during drying

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