Marquié C
Laboratory of Cotton Technology, CIRAD-CA-Technologie du coton, TA 70/16 Avenue Agropolis, 34398 Montpellier Cedex 5, France.
J Agric Food Chem. 2001 Oct;49(10):4676-81. doi: 10.1021/jf0101152.
Amino acids involved in cottonseed protein cross-linking by formaldehyde, glutaraldehyde, and glyoxal during protein film formation were identified by an original technique. The entire HPLC amino acid profile (after acid hydrolysis) was studied, along with variations in reactive lysine contents, in films cross-linked or not with increasing quantities of formaldehyde, glutaraldehyde, and glyoxal. This strategy highlighted the formation of acid-resistant lysine derivatives that a simple reactive lysine determination would not have detected. The results-which agree with previously published data-enhance the overall understanding of cross-linking activities that occur in aqueous alkaline solutions during the formation of protein films made with cottonseed flour. Lysine was found to have a key role in protein cross-linking by dialdehydes, with the involvement of tyrosine in the presence of formaldehyde and of arginine in the presence of glyoxal. These results could provide valuable chemical tools for adjusting the mechanical properties of cottonseed protein films.
通过一种原创技术鉴定了在蛋白质膜形成过程中，参与棉籽蛋白与甲醛、戊二醛和乙二醛交联的氨基酸。研究了完整的HPLC氨基酸谱（酸水解后），以及在与不同量甲醛、戊二醛和乙二醛交联或未交联的膜中反应性赖氨酸含量的变化。该策略突出了耐酸性赖氨酸衍生物的形成，而简单的反应性赖氨酸测定无法检测到这些衍生物。这些结果与先前发表的数据一致，增强了对在用棉籽粉制成的蛋白质膜形成过程中，在碱性水溶液中发生的交联活性的整体理解。发现赖氨酸在二醛介导的蛋白质交联中起关键作用，在甲醛存在下酪氨酸参与其中，在乙二醛存在下精氨酸参与其中。这些结果可为调节棉籽蛋白膜的机械性能提供有价值的化学工具。
