- Methods of treatment using water-soluble tryptophan-containing peptides obtained by the hydrolysis of hens eggs lysozyme
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The present invention relates to a process to produce a composition comprising water-soluble peptides and having a Trp/LNAA ratio of more than 0.15, which comprises hydrolyzing lysozyme, preferably hen eggs lysozyme, to prepare a hydrolysate having a DH of between 5 and 45.
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Page/Page column 19
(2016/01/25)
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- Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins
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A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.
- Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi
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supporting information; experimental part
p. 2327 - 2335
(2011/05/02)
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- Synthesis and separation of L-trytophan oligo-peptides assisted by phosphorus oxychloride
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With the assistance of inorganic phosphorus, α-amino acids could self-assemble into a series of oligopeptides, so it could provide a new route to synthesize peptides. In this paper, the self-assembly reaction of L-trytophan mediated by phosphorus oxychloride was monitored by using ESI-MS. The proper condition of the self-assembly reaction of L-Try was reported. The reaction products were purified by RP-HPLC and the fragmentation pathway for L-Try oligo-peptides were analyzed by using ESI-MS/MS.
- Ma, Li,Zhao, Dong-Xin,Ren, Hai-Ping,Lu, Kui,Zhao, Yu-Fen
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experimental part
p. 4393 - 4397
(2010/11/16)
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