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超高压处理对牛α-乳白蛋白结构的影响。

Effects of high hydrostatic pressure on the structure of bovine alpha-lactalbumin.

机构信息

Departamento de Graduados e Investigación en Alimentos, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Carpio y Plan de Ayala, CP. 11340 México, DF, México.

出版信息

J Dairy Sci. 2010 Apr;93(4):1420-8. doi: 10.3168/jds.2009-2786.

DOI:10.3168/jds.2009-2786
PMID:20338419
Abstract

The effects of high hydrostatic pressure (HHP) processing (at 200 to 600 MPa, 25 to 55 degrees C, and from 5 to 15 min) on some structural properties of alpha-lactalbumin was studied in a pH range of 3.0 to 9.0. The range of HHP processes produced a variety of molten globules with differences in their surface hydrophobicity and secondary and tertiary structures. At pH values of 3 and 5, there was a decrease in the alpha-helix content concomitant with an increase in beta-strand content as the pressure increased. No changes in molecular size due to HHP-induced aggregation were detected by sodium dodecyl sulfate-PAGE. All samples showed higher thermostability as the severity of the treatment increased, indicating the formation of a less labile structure related to the HHP treatment.

摘要

在 pH 值为 3.0 至 9.0 的范围内研究了高压处理(200 至 600 MPa,25 至 55°C,5 至 15 分钟)对α-乳白蛋白某些结构特性的影响。该高压处理范围产生了多种具有不同表面疏水性和二级及三级结构的变性球蛋白。在 pH 值为 3 和 5 时,随着压力的增加,α-螺旋含量降低,β-折叠含量增加。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳未发现由于高压诱导聚集而导致的分子大小变化。所有样品的热稳定性随着处理强度的增加而提高,表明与高压处理相关的形成了一种不太稳定的结构。

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