摘要
商品化的大豆分离蛋白(SPI)主要由7S和11S两种球蛋白组成,两者较难分离.同时,由于球蛋白的紧密结构使SPI难以直接溶解于水中.采用盐酸胍和二硫苏糖醇在溶解过程中对SPI进行处理,从而获得了较高浓度,并且蛋白质分子链未发生降解的SPI水溶液.此外,通过采用盐酸胍溶解和透析的方法,获得以7S球蛋白为主的溶液和以11S球蛋白为主的沉淀,比较简单地实现SPI中两种主要组份的初步分离.
Both solubility tests and reference data proved that commercially available soy protein isolate（SPI） had low solubility in pure water.As an alternative,guanidine hydroxyl chloride（GuHCl） and dithiothreitol（DTT） were used to treat SPI during the dissolution process.After dialysis of GuHCl and DTT,an SPI aqueous solution was obtained.Solubility tests showed this SPI aqueous solution had a relatively high concentration（6 times larger as that directly dissolved in pure water）,and sodium dodecyl sulfate-polyacrylamide gel electrophoresis（SDSPAGE） showed that such an SPI solution did not suffer the degradation of the protein subunits.In addition,through a simple treatment of GuHCl and dialysis process,a 7S-rich solution and an 11S-rich sediment were obtained,so that the two major components of SPI were primarily separated.SDS-PAGE gave the major evidence of the separation,and the possible mechanism of the separation was discussed.It was a relative simple method with high productivity,though the separation efficiency was lower than that of the chromatography method.The paper provides new insights into the role of disulfide bonds that play in stabilizing the structure of SPI,especially that of the component 11S.
出处
《高分子学报》
SCIE
CAS
CSCD
北大核心
2010年第2期250-254,共5页
Acta Polymerica Sinica
基金
国家自然科学基金(基金号20674011)
教育部新世纪优秀人才支持计划(项目号NCET-06-0354)
教育部长江学者和创新团队发展计划(项目号IRT-06-12)资助项目
