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KMID : 0380020100250040395
Korean Journal of Biotechnology and Bioengineering
2010 Volume.25 No. 4 p.395 ~ p.400
Glyceryl Esterification of Fibroin Peptide by Papain
Jeong Jae-Ho

Lee Shin-Young
Hur Won
Abstract
Papain hydrolysate of fibroin was found to be mainly composed of several even-numbered peptides that can be produced at a large scale and can be used as a precursor for biological fine-chemicals such as peptide detergents. Thus, the hydrolysate was further modified to synthesize a peptide mixture of glyceryl esters using the identical enzyme for the production of such chemicals. Formation of glyceryl ester of each peptide was confirmed by identifying peaks of the nominal mass shift of +74 Da in mass spectrometry. Analysis of the mass spectra indicated that glyceryl esters of di- and tetra-peptides were the major constituents of the mixture and that alanylglycine was most preferentially esterified. It also suggests that papain prefers dipeptide to tetrapeptide and alanine to serine or tyrosine at P2 position as substrate for glyceryl esterification. The glyceryl esters were recovered using ion exchange resin and the yield of glyceryl esterification recorded was 17.8% by weight.
KEYWORD
fibroin peptide, glyceryl ester, papain, peptidyl glyceride
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