The preparation of crystalline rennin and a study of some of its properties

Baun, Robert M. De; Connors, William M.; Sullivan, Royal A.

doi:10.1016/0003-9861(53)90128-3

Cited by 20 publications

(2 citation statements)

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“…This can be attributed to (1) a slightly lower casein concentration in the MPC samples compared with MCC; and (2) lower total calcium (Table 1) and free ionic calcium (Table 3) in MPC compared with MCC. The concentration of calcium ions is known to play a critical role in the nonenzymatic stage of milk coagulation (De Baun et al, 1953).…”

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Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates

Cadesky

Walkling-Ribeiro

Kriner

et al. 2017

Journal of Dairy Science

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Reconstituted micellar casein concentrates and milk protein concentrates of 2.5 and 10% (wt/vol) protein concentration were subjected to high-pressure processing at pressures from 150 to 450 MPa, for 15 min, at ambient temperature. The structural changes induced in milk proteins by high-pressure processing were investigated using a range of physical, physicochemical, and chemical methods, including dynamic light scattering, rheology, mid-infrared spectroscopy, scanning electron microscopy, proteomics, and soluble mineral analyses. The experimental data clearly indicate pressure-induced changes of casein micelles, as well as denaturation of serum proteins. Calcium-binding α- and α-casein levels increased in the soluble phase after all pressure treatments. Pressurization up to 350 MPa also increased levels of soluble calcium and phosphorus, in all samples and concentrations, whereas treatment at 450 MPa reduced the levels of soluble Ca and P. Experimental data suggest dissociation of calcium phosphate and subsequent casein micelle destabilization as a result of pressure treatment. Treatment of 10% micellar casein concentrate and 10% milk protein concentrate samples at 450 MPa resulted in weak, physical gels, which featured aggregates of uniformly distributed, casein substructures of 15 to 20 nm in diameter. Serum proteins were significantly denatured by pressures above 250 MPa. These results provide information on pressure-induced changes in high-concentration protein systems, and may inform the development on new milk protein-based foods with novel textures and potentially high nutritional quality, of particular interest being the soft gel structures formed at high pressure levels.

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confidence: 99%

Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates

Cadesky

Walkling-Ribeiro

Kriner

et al. 2017

Journal of Dairy Science

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“…In the calf also, gastric mucosal extracts have been shown to digest proteins with two pH maxima near 2 and 3.5 (Berridge, 1945). The second maximum is attributed, however, to rennin, which when crystallized from crude extracts undoubtedly digests proteins with a pH maximum near 3-5 (Berridge, 1945;De Baun, Connors & Sullivan, 1953). Rennin might thus seem to be taking the place of the 'cathepsin' of other mammals, but the absence of a second pH maximum from rennin-free extracts of calf gastric mucosa has never been demonstrated.…”

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Studies on gastric proteolysis. 1. The proteolytic activity of human gastric juice and pig and calf gastric mucosal extracts below pH 5

1959

Biochemical Journal

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STAPHYLOCOCCAL o-HAEMOLYSIN 73 3. The isoelectric point of the haemolytic factor was determined by an electrophoretic-fractionation method and found to be at pH 6-4. I would like to thank Professor S. D. Elek for his interest and for many valuable discussions. I am also grateful to Mr A. Coddington for certain of the nitrogen determinations, and to Miss J. Holmes, Miss S. Williams and Miss J. Goldston for technical assistance during the course of this work. REFERENCES

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Rennin and the Clotting of Milk

Nj¹

1954

Advances in Enzymology - And Related Areas of Molecular Biology

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The preparation of crystalline rennin and a study of some of its properties

Cited by 20 publications

References 20 publications

Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates

Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates

Studies on gastric proteolysis. 1. The proteolytic activity of human gastric juice and pig and calf gastric mucosal extracts below pH 5

Rennin and the Clotting of Milk

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