Poon S, Clarke A, Currie G, Schultz C
Cooperative Research Centrefor Bioproducts, School of Botany, University of Melbourne, Vic., Australia.
Biosci Biotechnol Biochem. 2001 Aug;65(8):1713-23. doi: 10.1271/bbb.65.1713.
A peptide derived from apomyoglobin by cyanogen bromide cleavage was found to be an active emulsifier. This molecule, peptide 1-55, has two potential amphipathic alpha-helices and a hydrophilic C-terminal domain. The importance of each of these domains to the emulsifying properties of this molecule was investigated by testing the products of gene constructs based on the sequence of peptide 1-55, but lacking one of the three domains. The emulsifying activity of the peptides lacking either of the alpha-helices was correlated with the hydrophobic moments of their respective helices. The hydrophobic moment is a measure of the amphipathicity of alpha-helices; a hydrophobic moment analysis of other emulsifying peptides supports the hypothesis that a high hydrophobic moment contributes to good emulsifying properties in a molecule which contains alpha-helices.
通过溴化氰裂解从脱辅基肌红蛋白衍生而来的一种肽被发现是一种活性乳化剂。该分子，即肽1-55，有两个潜在的两亲性α螺旋和一个亲水性C末端结构域。通过测试基于肽1-55序列但缺少三个结构域之一的基因构建体的产物，研究了这些结构域中每一个对该分子乳化特性的重要性。缺少任何一个α螺旋的肽的乳化活性与其各自螺旋的疏水矩相关。疏水矩是α螺旋两亲性的一种度量；对其他乳化肽的疏水矩分析支持这样一种假设，即在含有α螺旋的分子中，高疏水矩有助于良好的乳化特性。
