Extent of κ-casein hydrolysis during renneting of bovine milk: A critical assessment of the analytical and estimation approaches.

Renneting is an enzymatic process that turns milk into curd which is then transformed into cheese. Rennet-induced coagulation of caseins (CNs) is the critical step during this process and the key is the primary hydrolysis of κ-CN's Phe-Met bond by chymosin. This article comprehensively reviews the existing data on the extent/degree of κ-CN hydrolysis during renneting of bovine milk and critically evaluates its determination methods.

Structural dependence of concentrated skim milk curd on micellar restructuring.

This study was conducted to establish an understanding of how milk concentration modulates the rennet curd structure. Rennet-induced gelation and renneting under slow acidification achieved using glucono-δ-lactone (GDL) and structural properties of reconstituted skim milk gels at two concentration levels (9 and 25 % total solids) were studied by measuring variations in (a) viscoelastic behaviour, (b) micellar size, charge density, diffusivity, and (c) hydrophobicity using dynamic rheometry, dynamic light scattering and fluorimetry, respectively. Concentrated milk showed a greater estimated hydrodynamic radius of casein micelles, lower zeta (ζ)-potential, ratio of serum to total Calcium (Ca) and charge density and increased surface hydrophobicity, all supporting the view that micellar restructuring particularly sub-particle transfer takes place and contributes to rapid gelation.