z-logo
Premium
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
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom