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- W2067067295 abstract "Abstract Strong disulfide reducing agents Na 2 SO 3 and NaBH 4 increased nonprotein nitrogen (NPN) in the casein complex from sterile concentrated milk. The sulfur-containing reducing agents mercaptoethanol, thioglycolate, and cysteine reduced the disulfide linkages and decreased stabilities to Ca ++ of the casein complex, of whole and of κ-caseins with slight changes in NPN. Increasing pH to 12 with 0.1 N NaOH also split the linkages and decreased stability of whole and κ-caseins. Decreased stabilities were almost completely restored by air oxidation and neutralization. Degrading κ- and whole caseins with NaOH and NaBH doubled the sulfur compounds by the p-mercuribenzoate (PMB) method as compared to reducing them with Na 2 SO 3 . The sulfhydryl blocking agents PMB, N-ethylmalcimide (NEM), iodoacetamide, and Salyrgan retarded gelation and the disulfide-reducing agents mercaptoethanol, thioglycolate, cysteine, and glutathione promoted gelation of sterile concentrated milk and of α-casein with and without β-lactoglobulin in the presence of Ca ++ . β-Lactoglobulin accelerated gelation of α-casein. The effects of cystine and oxidized glutathione (GSSG) became evident only after long storage. α-Casein containing glutathione (GSH) gelled quicker, decreased in stability more than the control, and protein bound SH − increased and nonprotein SH − decreased during storage. Masked SH − groups were not found in either κ- or whole caseins." @default.
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- W2067067295 date "1965-04-01" @default.
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- W2067067295 title "Effect of Changes in Sulfur Compounds on Stability and Gelation of Caseins and of Sterile Concentrated Milk" @default.
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- W2067067295 doi "https://doi.org/10.3168/jds.s0022-0302(65)88248-0" @default.
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