Santhana Srinivasan
Center for Environmental Science and Technology,
Rolla, Missouri
Tanzania
Research Article
Efficacy of L-Cysteine as an Anti-Oxidant in Papain Catalyzed Synthesis of
Oligopeptides in Organic Solvent System
Author(s): Santhana Srinivasan, Shubhen Kapila, Daniel Forciniti and Paul NamSanthana Srinivasan, Shubhen Kapila, Daniel Forciniti and Paul Nam
Enzymatic peptide synthesis has drawn considerable attention for synthesis of high by-pass oligopeptide feed supplements in animal nutrition. A hardy protease, (papain) with a cysteine moiety at the active site requires the presence of an anti-oxidant in the reaction medium to ensure that the thiol group remains intact. Free cysteine has been the antioxidant of choice for papain-catalyzed synthesis of oligopeptides in aqueous systems. However, due to limited solubility of cysteine in organic solvents, it is generally not a suitable antioxidant for the synthesis of oligopeptides in biphasic solvent systems; instead, mercaptoethanol is often used. Lysine and Methionine is couple of well-known limiting amino acids that find application in cattle feed and poultry. Synthesis of co-oligopeptides of Lysine and Methionine has generally been attempted in bi-phasic solvent systems with Mercapto.. View More»
DOI:
10.4172/2161-1009.1000335