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Synthesis by enzymatic catalysis. III. Copolymerisation of amino acids and dipeptides using papain
Author(s) -
Selvi Christine,
Baboulene Michel,
Speziale Vincent,
Lattes Armand
Publication year - 1986
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280360906
Subject(s) - papain , dipeptide , tyrosine , chemistry , substrate (aquarium) , monomer , amino acid , polymerization , methionine , enzyme , catalysis , enzyme catalysis , peptide , amide , stereochemistry , organic chemistry , combinatorial chemistry , biochemistry , polymer , biology , ecology
Abstract After studying the oligomerisation reaction of L‐tyrosine, we investigated polymerisation of a mixture of methionine and tyrosine, which also led to the formation of a polypeptide. Various substrate concentrations and substrate/enzyme ratios were investigated. A hexapeptide was isolated containing three tyrosine and three methionine residues. Extension of the method to enzymatic polymerisation of dipeptide esters was also examined. After optimisation of the reaction, we obtained a peptide made up of four monomers using methyl L‐leucyl‐L‐tyrosinate as substrate. The results are discussed in the light of a possible reaction mechanism.