Abstract：
:Papain-catalyzed polymerization of L-tyrosine ethyl ester in aqueous media was efficient for synthesis of oligo-tyrosine peptides having angiotensin I-converting enzyme inhibitory activity. Di-, tri-, and tetra-tyrosine accumulated in the soluble fraction of reaction mixture. On the other hand, the peptide products with degree of polymerization from 5 to 10 were insoluble, yields of which were influenced by initial concentrations of the ester substrate. The precipitated products could be used as substrates for α-chymotrypsin in DMSO/buffer systems producing soluble oligo-tyrosine peptides. In the reaction media containing DMSO at 40-50% (v/v), most of the precipitates were converted to soluble peptides. The two-step enzymatic reaction, that is papain-catalyzed synthesis of Tyr-polymers from L-tyrosine ethyl ester followed by their hydrolytic cleavage by α-chymotrypsin, is expected to be a potent procedure for synthesis of biologically active di- and tri-tyrosine peptides in good yield.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Narai-Kanayama A,Shikata Y,Hosono M,Aso Kdoi
10.1016/j.jbiotec.2010.09.931subject
Has Abstractpub_date
2010-11-01 00:00:00pages
343-7issue
3eissn
0168-1656issn
1873-4863pii
S0168-1656(10)01840-7journal_volume
150pub_type
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