Trypsin and trypsin inhibitor bind milk beta-lactoglobulin: Protein-protein interactions and morphology

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• 作者：P. Chanphai ; H.A. Tajmir-Riahi ; ^{heidar-ali.tajmir-riahi@uqtr.ca}
• 关键词：b-LG ; beta-lactoglobulin ; FTIR ; Fourier transform infrared ; TEM ; transmission electron microscopy
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：754-758
• 全文大小：1295 K
• 卷排序：96

文摘

The conjugation of trypsin and trypsin inhibitor with milk b-LG is reported here. Protein–protein interactions are via H-bonding and van der Waals. Trypsin forms more stable aggregates than trypsin inhibitor. Major protein morphological changes are observed on protein–protein interactions. Conjugation induced major changes of b-LG structure, causing protein unfolding.