2000
DOI: 10.1002/(sici)1097-0010(200003)80:4<447::aid-jsfa547>3.0.co;2-z
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Protein stability function relations: native ?-lactoglobulin sulphhydryl-disulphide exchange with PDS

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Cited by 12 publications
(4 citation statements)
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References 49 publications
(47 reference statements)
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“…The formation of 2-thiopyridine (2-TP) was spectrophotometrically followed at 343 nm as a function of time. The equation for this second-order reaction has been published . The rate constant for pyridine disulfide reaction with protein ( k ) or GSH ( k *) is given in mole protein per second and was standardized by the rate constant for glutathione reaction with 2-pyridine disulfide determined under identical conditions and expressed as the sulfhydryl-disulfide exchange index (SEI).…”
Section: Experimental Methodsmentioning
confidence: 99%
“…The formation of 2-thiopyridine (2-TP) was spectrophotometrically followed at 343 nm as a function of time. The equation for this second-order reaction has been published . The rate constant for pyridine disulfide reaction with protein ( k ) or GSH ( k *) is given in mole protein per second and was standardized by the rate constant for glutathione reaction with 2-pyridine disulfide determined under identical conditions and expressed as the sulfhydryl-disulfide exchange index (SEI).…”
Section: Experimental Methodsmentioning
confidence: 99%
“…According to Dalgleish (1990), denaturation of whey proteins is a complex process: disulfide-linked aggregates are formed between serum proteins themselves at first denaturation stages. Apenten & Galani (2000) reported that this reaction may take place even at room temperature, but its extent increases with increasing temperature. This interaction could explain the reduction of SH groups when whey is heated at the lowest temperatures, while at the highest temperature (85°C), the complete denaturation of whey proteins leads to an increase of reactive SH groups, possibly by releasing them as a part of small molecules (Jiménez-Guzmán et al 2002).…”
Section: Sh Groups Levelmentioning
confidence: 99%
“…17,18 Exposure of nonpolar groups leads to increased hydrophobic interactions between surface-denatured protein molecules, 19 whereas exposure of sulfur-containing groups leads to disulfide bond formation or disulfide interchange reactions at neutral pH. 17,20 In the absence of salt, the increased hydrophobic attraction between the emulsion droplets is insufficient to promote flocculation because of the relatively strong electrostatic repulsion. On the other hand, in the presence of sufficient salt the electrostatic repulsion is screened and the hydrophobic attraction is large enough to promote droplet flocculation.…”
Section: Introductionmentioning
confidence: 99%