Physicochemical and structural characterisation of protein isolate, globulin and albumin from soapnut seeds (Sapindus mukorossi Gaertn.)
文献类型: 外文期刊
第一作者: Yin, Shou-Wei
作者: Yin, Shou-Wei;Tang, Chuan-He;Yang, Xiao-Quan;Wen, Qi-Biao;Qi, Jun-Ru;Yin, Shou-Wei;Chen, Ji-Cheng;Chen, Ji-Cheng;Sun, Shang-De
作者机构:
关键词: soapnut (sapindus mukorossi gaertn.);physico-chemical property;conformation;globulin;albumin;protein isolate
期刊名称:FOOD CHEMISTRY ( 影响因子:7.514; 五年影响因子:7.516 )
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年卷期:
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收录情况: SCI
摘要: The amino acid (AA) composition and physicochemical and conformational properties of protein isolate (SNP1), globulin (SNG) and albumin (SNA) fractions from soapnut seeds were evaluated. The essential AA of SNG, SNA and SNPI (except sulfur-containing AA) are sufficient for the FAO/WHO suggested requirements for 2-5 year old infants. SNG and SNPI showed similar electrophoresis patterns and AA compositions, the subunit of those proteins consisted of two polypeptides linked by disulfide bonds. In contrast, SNA showed a different AA compositions and SDS-PAGE pattern. Both SNG and SNPI presented a typical U-shape protein solubility (PS)-pH profile, SNA showed a completely different PS-pH profile, especially at pH 2.0-4.0. The near-UV circular dichroism (CD), differential scanning calorimetry (DSC) and trypto-phan fluorescence spectra analyses indicated that the flexibility in tertiary conformations decreased in the order: SNA > SNPI > SNG, while soapnut proteins had a similar secondary conformation, with a highly ordered structure (the (5-types), as evidenced by far-UV CD spectra.
分类号: TS2
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