ISSN:
1573-6776
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary Esterification of dipeptide was performed with papain immobilized on XAD-7 with methylene chloride as the organic solvent. The esterification of a peptide substrate Box-X-Y-OH is promoted by the presence of a hydrophobic aminoacid residue (e.g., Phe, Leu) in the X (P2) position. Good yields were observed for example with Boc-Phe-Glu-OH and Boc-Ala-Glu-OH. With a hydrophilic aminoacid residue in the X position no esterification of the dipeptide takes place. Instead hydrolysis of the peptide bond occurs. This is also the case with glycine as the aminoacid; for instance Boc-Leu-Gly-OH gives a 80% yield of esterification whereas Boc-Gly-Leu-OH gives only the aminoester Boc-Gly-OR.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01026648
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