Action of rennin on heat-sterilized milk

Hindle, E J; Wheelock, J. V.

doi:10.1042/bj1150019pb

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1980

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Cited by 3 publications

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“…The composition of the carbohydrate part has been studied (33,210), and different minor components shown to have different proportions of the various carbohydrate residues (211). The attachment of most of the glycosidic residues is probably to asparagine-45 (34); glyco-a-lactalbumin is as effective as a-lactalbumin in the lactose synthetase reaction (33).…”

Section: Primary Structurementioning

confidence: 99%

Section C. Chemistry of milk proteins

Lyster¹

1972

Journal of Dairy Research

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Section: Primary Structurementioning

confidence: 99%

Section C. Chemistry of milk proteins

Lyster¹

1972

Journal of Dairy Research

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Psychrotrophic Bacteria cause Changes in Stability of Milk to Coagulation by Rennet or Heat

Cousin

Marth

1977

Journal of Dairy Science

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Effects of Small Concentrations of Mucor miehei Protease on Stability of Sterile Milk-Based Dietetic Foods

Thunell

Ernstrom

Hartman

1980

Journal of Dairy Science

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Four commercial sterile milk-based dietetic products were inoculated aseptically with small concentrations of a commericial milk clotting enzyme derived from Mucor miehei and incubated at 30 C for 32 wk. One of the products, Sustacal, exhibited no observable changes in body and texture during storage. Enzyme concentrations of 1 x 10(-4) chymosin units per milliliter or higher induced undesirable changes in the body of the other three products, Enfamil Ready-to-Use, Enfamil Concentrate, and Metrecal Shape. None of the products was affected visibly by enzyme concentrations of 1 x 10(-5) chymosin units per milliliter or less. In-can sterilization of Enfamil Ready-to-Use at 126.1 C for 4.5 min and Enfamil Concentrate at 126.7 C for 4.23 min completely destroyed all measurable enzyme activity at concentrations (up to 5.5 x 10(-2) chymosin units per milliliter) in these experiments. However, 1 to 3 h between formulation and sterilization allowed time for the enzyme at concentrations of 1 x 10(-2) chymosin units per milliliter or more to cause coagulation during heat sterilization.

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Action of rennin on heat-sterilized milk

Cited by 3 publications

References 4 publications

Section C. Chemistry of milk proteins

Section C. Chemistry of milk proteins

Psychrotrophic Bacteria cause Changes in Stability of Milk to Coagulation by Rennet or Heat

Effects of Small Concentrations of Mucor miehei Protease on Stability of Sterile Milk-Based Dietetic Foods

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