Enzymatic Synthesis and Characterization of L-Methionine and 2-Hydroxy-4-(methylthio)butanoic Acid (HMB) Co-oligomers
Oligomers of l-methionine (Met) and its hydroxy analogue, 2-hydroxy-4-(methylthio)butanoic acid (d,l-HMB) were synthesized with the proteolytic enzyme papain. The Met homooligomers and HMB−Met co-oligomers obtained through the enzymatic reactions were subjected to persulfonation and separated with reverse phase liquid chromatography (RPLC). The separated oligomers were characterized with electrospray ionization-mass spectrometry (ESI-MS). The oligomers were also characterized with matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS). The results showed that co-oligomers were predominantly composed of 4−8 Met residues and one HMB residue. The data also suggest that in the co-oligomers, HMB is attached at the N-terminal end of the oligopeptide chain.
M. Rajesh et al., "Enzymatic Synthesis and Characterization of L-Methionine and 2-Hydroxy-4-(methylthio)butanoic Acid (HMB) Co-oligomers," Journal of Agricultural and Food Chemistry, American Chemical Society (ACS), Mar 2003.
The definitive version is available at http://dx.doi.org/10.1021/jf026093g
Chemical and Biochemical Engineering
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