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酪蛋白胶束稳定性的CPG色谱研究。

CPG-chromatography studies of the stability of casein micelles.

作者信息

Larsson-Raźnikiewicz M, Almlöf E, Ekstrand B

出版信息

J Dairy Res. 1979 Apr;46(2):313-6. doi: 10.1017/s0022029900017222.

Abstract

Casein micelles fractionated on controlled pore glass (CPG-10/3000) were shown to be stable by recycling experiments. Only minor effects on the size distribution of the casein micelles were found after heating skim-milk to 100 degrees C for 10 min, or freeze-drying skim-milk at -70 degrees C followed by resuspension in the synthetic milk serum of Jenness & Koops (1962). The heating caused some whey proteins (beta-lactoglobulin) to enter the micelle fractions while the freeze-drying caused some of the largest micelles to disrupt. In colloidal calcium phosphate-free skim-milk prepared according to Pyne & McGann (1960) all the micelles appeared to dissociate into monomeric caseins.

摘要

通过循环实验表明,在可控孔径玻璃(CPG - 10/3000)上分级分离的酪蛋白胶束是稳定的。将脱脂乳加热至100℃持续10分钟,或将脱脂乳在-70℃下冷冻干燥,然后再悬浮于Jenness和Koops(1962)的合成乳清中后,发现对酪蛋白胶束的尺寸分布只有轻微影响。加热使一些乳清蛋白(β-乳球蛋白)进入胶束部分,而冷冻干燥则导致一些最大的胶束破裂。在按照Pyne和McGann(1960)制备的无胶体磷酸钙脱脂乳中,所有胶束似乎都解离成单体酪蛋白。

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