Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Role of β-Casein in Milk Curdling
Se-Eok YUNKunio OHMIYAShoichi SHIMIZU
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JOURNAL FREE ACCESS

1982 Volume 46 Issue 2 Pages 443-449

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Abstract

The tension values were determined for milk curds formed by six protéases using a curd tension meter. In curds with relatively high tension values, which were prepared by rennet, Mucor rennin and pepsin (acid proteases), αs- and β-casein were negligibly hydrolyzed during incubation after clotting, whereas both casein fractions in the fragile curds prepared by Alkaline-protease from Bacillus subtilis, trypsin and thermolysin (alkaline proteases) were electrophoretically degraded during further incubation after clotting. This phenomenon was more prominent in the β-casein fraction. However, when alkaline proteases were employed in an immobilized form and removed from the test-milk at the initiation of clotting, the degradation of β-casein was decreased, and curd tension values were increased. Inhibition of the enzymatic degradation of β-casein by addition of sodium chloride (5%) led to an increase in curd tension. When the test-milk treated by each immobilized alkaline protease was fortified with β-casein, curd tension value increased significantly. These results suggest that β-casein might be essential for the hardening of curd.

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