Section C. Chemistry of milk proteins

Lyster, R. L. J.

doi:10.1017/s0022029900014114

Cited by 93 publications

(11 citation statements)

References 402 publications

(351 reference statements)

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“…It was reported by Andrews & Cheeseman (1971,1972 and by Andrews (1975) that during storage of ultra-heat-treated (UHT) milk chemical reactions take place which lead to altered electrophoretic behaviour, loss in amino-N and an increase in the polymerized fraction of milk proteins consistent with the involvement of lysine residues and lactose in Maillard type reactions which are known to occur in other milk products during storage (Henry et al 1948).…”

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confidence: 99%

Chemical changes in ultra-heat-treated milk during storage: I. Hydrolysis of casein by incubation with pronase and a peptidase mixture

Möller¹,

Andrews²,

Cheeseman³

1977

Journal of Dairy Research

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Casein samples from untreated milk and stored ultra-heat-treated (UHT) milk were hydrolysed with pronase (protease ex Streptomyces griseus K-l) and subsequently with a mixture of peptidases prepared from the microsomal fraction of hog kidneys. Incubation of casein from unheated milk with pronase alone hydrolysed 70-80% of peptide bonds involving He, Leu, Tyr, Phe and His residues; other amino acids were released less well and proline hardly at all. The pronase/peptidase treatment resulted in 90-100% hydrolysis of peptide bonds involving all amino acids, including proline.Caseins from stored UHT milks were more resistant to proteolysis than casein from unheated milk. Reduced release of all amino acids was observed from samples taken after storage at 37 °C for 12 months or longer and for Lys, Arg and Asn residues from samples taken after storage at 30 °C for 14 months. Resistance to proteolysis was attributed to the Maillard reaction between milk proteins and lactose during storage of UHT milk.

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confidence: 99%

Chemical changes in ultra-heat-treated milk during storage: I. Hydrolysis of casein by incubation with pronase and a peptidase mixture

Möller¹,

Andrews²,

Cheeseman³

1977

Journal of Dairy Research

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“…(i) Whey proteins. Several authoritative books and reviews on milk proteins discuss the occurrence, origins, structure,~nd functions of the whey proteins, Lyster (1972), WhItney (1976), McKenzie (1971. It is usual to divide.…”

Section: Composition Of Wheymentioning

confidence: 99%

Whey research

Evans¹

1980

Int J of Dairy Tech

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The composition of whey is briefly discussed and less well‐known areas for research on whey are highlighted. On whole whey solids aspects of lactose intolerance and of whey taint require attention. Lactose derivatives, the flavour‐binding quality of lactose, and its precise behaviour in dough require sudy. A long‐shot application for binding fines in steelmaking forms the subject of an American specification. Whey proteins, with or without chemical or physical modification, in human foods require study of functional properties. The high nutrient density of whey proteins suit them for the so‐called prudent diet foods. The importance of lactoperoxidase as part of a bactericidal system in the gut of neonates is stressed. Further research is required on fractionation of proteins by membrane processes and ion‐exchange.

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“…The four bovine /?-lactoglobulins consist of two identical polypeptide chains of 18 000 daltons with only a few aminoacid substitutions (LYSTER, 1972). Their aminoacid sequence is known (BRAU-NITZER er a]., 1972), but not their conformation.…”

Section: Soci6tg Belge De Biochimiementioning

confidence: 99%