Relation of Heat-induced Changes in Protein-salt Constituents to Astringency in Milk Systems

摘要: Abstract Selected milk systems were heated at varying levels and subsequently examined for astringent flavor response, as well by high speed centrifugation, Sephadex gel filtration, polyacrylamide electrophoresis, electron microscopy, chemical analyses, to determine changes in the size, shape, composition of protein-salt aggregate particles present. Astringency was produced heating various skimmilk, whey, ultrafiltrate systems. development whey accompanied aggregation formation large salt particles, respectively. Heating skimmilk produce astringency resulted association calcium phosphate proteins with caseinate system without noticeably altering or density caseinate-phosphate micelles. Although particle size is not sole factor related astringency, it appears that components associated must attain critical colloidal dimensions, impart response. The effective nature heat-altered constituents their micelles are indicated primary origin milk.