High level production of bioactive di- and tri-tyrosine peptides by protease-catalyzed reactions.
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.
Narai-Kanayama
Asako
A
Faculty of Applied Life Science, Nippon Veterinary and Life Science University, 1-7-1 Kyonan-cho, Musashino-shi, Tokyo 180-8602, Japan.
Shikata
Yasuhiro
Y
Hosono
Masumi
M
Aso
Keiichi
K
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D019149:Bioreactors; D001709:Biotechnology / Q000379:methods*; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism*; D004121:Dimethyl Sulfoxide / Q000737:chemistry; D010206:Papain / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis / Q000737:chemistry / Q000378:metabolism
D000806:Angiotensin-Converting Enzyme Inhibitors; C101095:trityrosine; D014443:Tyrosine; C007543:dityrosine; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D010206:Papain; D004121:Dimethyl Sulfoxide