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.
Rajesh
Mathur
M
Center for Environmental Science and Technology and Department of Chemistry, University of Missouri-Rolla, 1870 Miner Circle, Rolla, Missouri 65409-0530, USA.
Kapila
Shubhen
S
Nam
Paul
P
Forciniti
Daniel
D
Lorbert
Stephen
S
Schasteen
Charles
C
D002851:Chromatography, High Pressure Liquid / Q000379:methods; D013058:Mass Spectrometry / Q000379:methods; D008715:Methionine / Q000031:analogs & derivatives* / Q000032:analysis* / Q000096:biosynthesis; D010206:Papain / Q000378:metabolism*
C008391:alpha-hydroxy-gamma-methylmercaptobutyric acid; D008715:Methionine; D010206:Papain