“…The decrease in sulfhydryl groups with a concomitant oxidation resulted in the formation of disulfide bonds through oxidation of sulfhydryl groups or disulfide inter changes (Hayagawa and Nakai, 1985). Changes in SH groups are an indication of either the formation of disulfide bond or fresh exposure of reactive SH groups to the bulk solvent from the interior of the protein molecule (Murthy et al, 2012).…”
Section: Total Sulfhydryl Content Of Mfp Of Eelmentioning
confidence: 99%
“…4). Gel forming ability of fish proteins is an important functional property (Murthy et al, 2012). Benjakul et al, (2003) observed that the degradation of myosin results in an inferior gel network formation, causing a lower elasticity with poor water holding capacity in the gel matrix.…”
Section: Gel Strength Of Muscle Proteins Of Mfp Of Eel Fishmentioning
“…The decrease in sulfhydryl groups with a concomitant oxidation resulted in the formation of disulfide bonds through oxidation of sulfhydryl groups or disulfide inter changes (Hayagawa and Nakai, 1985). Changes in SH groups are an indication of either the formation of disulfide bond or fresh exposure of reactive SH groups to the bulk solvent from the interior of the protein molecule (Murthy et al, 2012).…”
Section: Total Sulfhydryl Content Of Mfp Of Eelmentioning
confidence: 99%
“…4). Gel forming ability of fish proteins is an important functional property (Murthy et al, 2012). Benjakul et al, (2003) observed that the degradation of myosin results in an inferior gel network formation, causing a lower elasticity with poor water holding capacity in the gel matrix.…”
Section: Gel Strength Of Muscle Proteins Of Mfp Of Eel Fishmentioning
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