Spectrofluorometric Determination of Sulfhydryl Groups in Cottage Cheese

Vakaleris, D.G.; Pofahl, T.R.

doi:10.3168/jds.s0022-0302(68)87151-6

Cited by 3 publications

(1 citation statement)

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“…Presence of -SH groups in isolated casein sample from boiled milk and khoa is due to heat induced entrapped whey proteins indicating heat induced casein-whey interactions. Vakaleris and Pofahl (1968) reported 3 times higher measurable -SH groups in high heat skim milk cheese as compared to pasteurized milk cheese. Since pasteurized milk curd is entirely casein, which has theoretically almost zero or very low measurable -SH groups therefore any significant amount of -SH in pasteurized cheese curd was due to the presence of whey proteins trapped in the curd.…”

Section: Sulfhydryl Contentmentioning

confidence: 97%

Effect of type and quality of milk on heat induced protein–protein interactions in khoa

et al. 2018

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The present study was carried out to evaluate the effect of developed acidity and subsequent neutralization of milk (cow/buffalo) on heat induced protein-protein interactions occurring at various stages during preparation. Protein-protein interactions were studied in terms of surface hydrophobicity (F), sulfhydryl (-SH) group and SDS PAGE. As milk progressed to boiling stage, increase in F and decrease in -SH content was observed. prepared from cow milk had comparatively higher values for F and lower values for -SH group. F was observed to be highest in acidic samples followed by neutralized and fresh samples. While considering -SH group, maximum values were observed in neutralized samples followed by acidic and fresh samples of both milk and . However, no visible difference was observed in SDS PAGE patterns of casein fractions isolated from different types of samples. The bands of β-lg and α-la did not resolve clearly in the samples due to high heat treatment involved in its preparation, indicating intense denaturation of whey proteins especially in neutralized samples where an alkaline medium resulted in strong binding between casein and whey proteins. The quality of milk also resulted in altered heat induced protein-protein interactions in .

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Section: Sulfhydryl Contentmentioning

confidence: 97%

Effect of type and quality of milk on heat induced protein–protein interactions in khoa

et al. 2018

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Studies on thermal treatment of hake Part 1. Effects of thermal treatment and frozen storage on the content of SH groups and rheologic properties of hake flesh

Seidler¹,

Lachowicz²,

Krupska³

1986

Nahrung

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Effects of frozen storage (3-8 months at -28 "C) and heating temperatures (40, 60, 80, 100, 120 and 130 "C) on SH groups content and minced meat hardness of the Pacific hake (Merluccius productus) were studied. Of the two factors under study, temperature effects proved dominating, both on the SH dynamics and on hardness. The duration of frozen storage did not influence the maximum content of SH groups: it affected only the location of the peak of the thiol groups contents temperature curve. Additionally, a high correlation between the SH content and hardness was found as a function of heating temperature: the correlation. however, became weaker with frozen storage time.

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Fluorometric Determination of Sulfhydryl and Disulfide Groups in Whey from Milk Processed by Turbulent Flow Ultra-High Temperature Processes

Senter¹,

Stone²,

Wenzl³

1973

Journal of Dairy Science

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Spectrofluorometric Determination of Sulfhydryl Groups in Cottage Cheese

Cited by 3 publications

References 1 publication

Effect of type and quality of milk on heat induced protein–protein interactions in khoa

Effect of type and quality of milk on heat induced protein–protein interactions in khoa

Studies on thermal treatment of hake Part 1. Effects of thermal treatment and frozen storage on the content of SH groups and rheologic properties of hake flesh

Fluorometric Determination of Sulfhydryl and Disulfide Groups in Whey from Milk Processed by Turbulent Flow Ultra-High Temperature Processes

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