渗滤
乳糖
脱脂牛奶
化学
热稳定性
酪蛋白
尿素
超滤(肾)
色谱法
离解(化学)
食品科学
材料科学
生物化学
微滤
膜
复合材料
物理化学
作者
Shane V. Crowley,Mathilde Megemont,Inge Gazi,Alan L. Kelly,Thom Huppertz,James A. O’Mahony
标识
DOI:10.1016/j.idairyj.2014.03.005
摘要
Milk protein concentrates (MPCs) were manufactured from skim milk at pilot scale by ultrafiltration, or ultrafiltration and diafiltration, to different protein concentration factors. MPCs were then spray-dried into seven powders ranging from 36.6% (w/w; MPC35) to 89.6% (w/w; MPC90) protein in dry matter. Powders were reconstituted to 3.5% (w/w) protein and the heat stability of MPC suspensions measured at 140 °C in the pH range 6.3–7.3. At pH < 6.8, the heat stability of MPC suspensions decreased with increasing protein content of the MPC powders, due to high Ca-ion activity. At pH > 6.8, the destabilising influence of increased Ca-ion activity with increasing protein content of the MPC powders was countered partially by reduced heat-induced κ-casein dissociation. The heat stability of MPC80 was restored by re-establishment of the serum composition of skim milk; fortification with lactose or urea only affected heat stability outside the pH region where rapid Ca-induced coagulation occurred.
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