有限胰蛋白酶水解对种子11S球蛋白理化和结构特征的比较影响

Comparative effects of limited tryptic hydrolysis on physicochemical and structural features of seed 11S globulins.

作者信息

Braudo E E, Danilenko A N, Guslyannikov P V, Kozhevnikov G O, Artykova G P, Lapteva N A, Vaintraub I A, Sironi E, Duranti M

机构信息

NM Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Food Chemistry and Biotechnology, Kosygin St 4, Moscow, Russia.

出版信息

Int J Biol Macromol. 2006 Nov 15;39(4-5):174-8. doi: 10.1016/j.ijbiomac.2005.12.006. Epub 2006 Jun 19.

DOI:10.1016/j.ijbiomac.2005.12.006

PMID:16787660

Abstract

The effect of the limited proteolysis by trypsin on selected seed storage 11S globulins (broad bean and pea legumins, glycinin and helianthinin) was studied by high-sensitive differential scanning calorimetry, fluorescence spectroscopy and analysis of proteolysis kinetics. Different behaviour of glycinin and helianthinin, on one hand, and broad bean and pea legumins, on the other, were observed: in the first group changes in the physicochemical characteristics of the proteins due to their limited proteolysis are more pronounced in comparison with the second one, in relation with the extent of primary structure modifications. The differences observed have been evaluated in relation with the amino acid sequence features of the four 11S globulin studied and agree with the literature data concerning the protein structural changes in the course of the limited proteolysis.

摘要

通过高灵敏度差示扫描量热法、荧光光谱法和蛋白水解动力学分析，研究了胰蛋白酶有限水解对选定的种子贮藏11S球蛋白（蚕豆和豌豆豆球蛋白、大豆球蛋白和向日葵球蛋白）的影响。观察到大豆球蛋白和向日葵球蛋白与蚕豆和豌豆豆球蛋白的不同行为：与第二组相比，第一组中由于有限水解导致的蛋白质物理化学特性变化更为明显，这与一级结构修饰的程度有关。所观察到的差异已根据所研究的四种11S球蛋白的氨基酸序列特征进行评估，并与有关有限水解过程中蛋白质结构变化的文献数据一致。