Ball-milling changed the physicochemical properties of SPI and its cold-set gels
Ball-milling changed the physicochemical properties of SPI and its cold-set gels
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球磨改变了 SPI 及其冷凝凝胶的理化性质
DOI：
10.1016/j.jfoodeng.2016.10.006
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发表时间：
2017-02-01
影响因子：
5.5
通讯作者：
Hu, Hao
中科院分区：
文献类型：
--
作者：
Liu, Bohui;Wang, Hui;Hu, Hao
在本研究中，研究了球磨（BM，Mixer Mill MM 400）处理对大豆分离蛋白（SPI）及其由葡萄糖酸-δ-内酯诱导的冷凝固凝胶的理化性质的影响。 BM处理4分钟后，SPI的BM显着增加了冷凝凝胶的凝胶强度和持水能力。BM处理没有改变SPI的一级结构，但引起二级结构的微小变化。此外，BM处理10分钟后，SPI的表面疏水性从2058逐渐增加到5051，而游离SH基团从3.92减少到2.65μmol/g蛋白质。此外，近UV CD光谱表明，三级构象稳定性增加，疏水基团可能转移到更疏水的微环境。 总之，适当的 BM 处理可以改变 SPI 的理化性质，并提高 SPI 冷置凝胶的凝胶性能。 (C) 2016 Elsevier Ltd. 保留所有权利。
In this study, the effect of ball-milling (BM, Mixer Mill MM 400) treatments on the physicochemical properties of soybean protein isolate (SPI) and its cold-set gels induced by glucono-delta-lactone was studied. BM of SPI increased the gel strength and" water holding capacity of cold-set gels significantly after 4 min of BM treatments. BM treatments did not alter the primary structure of SPI, but caused minor changes of the secondary structure. Furthermore, surface hydrophobicity of SPI increased gradually from 2058 to 5051 after 10 min of BM, while free SH groups reduced from 3.92 to 2.65 mu mol/g protein. Moreover, near-UV CD spectra indicated that the tertiary conformation stability was increased and the hydrophobic groups might shift to a more hydrophobic microenvironment. In conclusion, appropriate BM treatments could change the physicochemical properties of SPI and increased the gelation properties of SPI cold-set gels. (C) 2016 Elsevier Ltd. All rights reserved.