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Surface Hydrophobicity of _s1 -I, _s1 -Casein A and B and Its Implications in Cheese Structure

Department of Food Science and the Cheese Research Institute, University of Wisconsin-Madison, Madison 53706

ABSTRACT

The first major proteolytic cleavage during Cheddar cheese maturation is the scission of _s1-casein to give a small peptide and _s1-I. Previously this proteolytic step was correlated with changes in the rheological properties of cheese, notably a lower elasticity and a decrease in the force required to fracture the cheese. Using cis-parinaric acid and 1,8-anilinonaphthalene sulfonate, we showed that _s1-I and _s1-casein A have lower surface hydrophobicities than _s1-casein B. The peptide segment involving residues 14 to 24 of the _s1-casein B sequence must be important in the formation of a hydrophobic interaction site, and an extensive network of hydrophobically bonded _s1-casein molecules is probably important in young cheese as well as in concentrated casein solutions.

¹ On leave from the New Zealand Dairy Research Institute, Palmerston North.

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