Submitted to: Meeting Abstract
Publication Type: Proceedings
Publication Acceptance Date: June 28, 2007
Publication Date: July 2, 2007
Citation: Nunez, A., Qi, P.X. 2007. Study of Intermediate Products from the Cross-linking Reactions of Genipin with Beta-Lactoglobulin and Related Peptides by MALDI-TOF/TOF Mass Spectrometry. Proceedings of the 55th ASMS Conference on Mass Spectrometry. Technical Abstract: Genipin, methyl-1R,2R,6S-2-hydroxy-9-(hydroxymethyl)-3-oxabicyclo[4.3.0]nona-4,8-diene-5-carboxylate, is an aglycone derivative from geniposide found in the Gardenia jasminoides fruits, obtained through enzymatic hydrolysis with beta-glucosidase. Genipin has been shown to be capable of cross-linking proteins, such as gelatin, comparable to the traditional cross-linking agent glutaraldehyde, but it is 10,000x less cytotoxic. Genipin has been recognized for its potential applications in biomedical engineering and pharmaceutical industries. It reacts with primary amines, the episilon-amino groups of lysine in proteins, and to a lesser extent arginine and glutamine. However, the mechanism of this cross-linking reaction remains is not fully understood. In this study we examine the reactions of the tryptic peptides of beta-lactoglobulin and other synthetic peptides with genipin using mass spectrometry. The results provides evidences for reaction intermediates controlling the cross linking of proteins by genipin. The information is valuable in order to establish reaction conditions that will efficiently direct the cross linking process for the utilization of proteins obtained from surplus milk production into novel food and non-food products.