High level production of bioactive di- and tri-tyrosine peptides by protease-catalyzed reactions

Narai-Kanayama, Asako; Shikata, Yasuhiro; Hosono, Masumi; Asō, K.

doi:10.1016/j.jbiotec.2010.09.931

Cited by 18 publications

(16 citation statements)

References 31 publications

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“…Bioactive peptides can also be produced by chemical (in an almost non-aqueous phase) and enzymatic synthesis, and with the use of recombinant DNA methods [Minkiewicz and Dziuba 2009]. Synthesis is the most popular method of obtaining bioactive peptides in a laboratory [Narai-Kanayama et al 2010]. In industrial applications, foods containing bioactive peptides are produced by hydrolysis with the involvement of digestive proteolytic enzymes and proteolytic enzymes of microbiological origin [Korhonen and Pihlanto 2006].…”

Section: Strategy For Isolating and Analysing Bioactive Peptidesmentioning

confidence: 99%

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Dziuba

2014

Acta Sci Pol Technol Aliment

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Proteins are one of the primary components of the food, both in terms of nutrition and function. They are main source of amino acids, essential for synthesis of proteins, and also source of energy. Additionally, many proteins exhibit specifi c biological activities, which may have effect on functional or pro-health properties of food products. These proteins and their hydrolysis products, peptides, may infl uence the properties of food and human organism. The number of commercially available food products containing bioactive peptides is very low, apart from that milk proteins are their rich source. It could be supposed that number of available products with declared activity will rise in near future because of observed strong uptrend on interest in such products. Molecular and biological properties of milk proteins, as precursors of bioactive peptides was characterised in the work. Therefore, the strategy of research and obtaining of such peptides both in laboratory and industrial scale, as well as the range of their commercial application, was presented. Several examples of research efforts presenting high potential to develop new products containing bioactive peptides from milk proteins and predetermined as nutraceuticals was described.

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Section: Strategy For Isolating and Analysing Bioactive Peptidesmentioning

confidence: 99%

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Dziuba

2014

Acta Sci Pol Technol Aliment

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“…Overall, these two reactions were carried out at 25 • C and pH 7.5. Starting with 100 mM of Tyr-OEt, the final reaction products contained di-and tri-Tyr peptides in good yield, reaching 65% on an initial ester substrate basis [23]. Each of these two oligo-Tyr peptides exhibited a mixture of competitive and noncompetitive inhibitions of ACE from rabbit lung, with IC 50 values of 34 M and 48 M, respectively [21].…”

Section: Introductionmentioning

confidence: 99%

“…With respect to the efficient synthesis of Tyr-Tyr, NaraiKanayama et al [23] previously proposed the two-step enzymatic reaction, in which papain (EC 3.4.22.2)-catalyzed synthesis of Tyrpolymers from l-tyrosine ethyl ester (Tyr-OEt) in a buffer solution [24] was followed by their hydrolytic cleavage by ␣-chymotrypsin (EC 3.4.21.1) in aqueous DMSO media [23]. Overall, these two reactions were carried out at 25 • C and pH 7.5.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of papain-catalyzed synthesis of oligo-tyrosine peptides

Mitsuhashi

Nakayama

Narai-Kanayama

2015

Enzyme and Microbial Technology

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“…10,[16][17][18][19][20] Importantly, this method offers advantages over other processes because it requires limited or no side-chain protection of amino acids. 21 In addition, this alternative uses mild conditions and retains stereospecificity.…”

Section: Introductionmentioning

confidence: 99%

“…In such cases, the molecular weight of the polypeptide can be limited to a certain extent. 10,21 In contrast, an exopeptidase only cleaves terminal peptide bonds. Therefore, we assume that a decrease in the molecular weight of the synthesized polypeptide during the reaction could be avoided.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of peptides with narrow molecular weight distributions via exopeptidase-catalyzed aminolysis of hydrophobic amino-acid alkyl esters

Nitta

Komatsu

Ishii

et al. 2016

Polym J

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A new synthesis technique that produces homogeneous oligopeptides that are essential for the formation of self-assembled structures is described. In contrast with endopeptidases, exopeptidases, which catalyze the cleavage of terminal peptide bonds, can potentially prevent unexpected hydrolysis during aminolysis. This is the first report on exopeptidase-catalyzed oligopeptide synthesis. Oligo(L-leucine) was synthesized using the exopeptidase carboxypeptidase Y (CPDY), which also prevented enzymatic hydrolysis. A high yield of oligo(L-leucine) with a narrow polydispersity (PDI) was obtained by limiting polypeptide cleavage during aminolysis. The reaction conditions, such as the temperature, pH, CPDY and substrate concentrations, were optimized to produce the best yields, molecular weights and PDI of the oligomers. Hydrophobic L-leucine methyl ester and L-isoleucine methyl ester were found to be the appropriate substrates for CPDY-catalyzed oligomerization; however, no oligomers were obtained using hydrophilic amino-acid esters. Oligomer yields were also affected by the amino-acid ester groups. Remarkably, the PDI of the oligomers was as low as 1.0, regardless of the reaction conditions and types of substrates used. Thus, exopeptidase-catalyzed oligomerization may become an alternative route for the current endopeptide-catalyzed oligomerization of peptides.

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High level production of bioactive di- and tri-tyrosine peptides by protease-catalyzed reactions

Cited by 18 publications

References 31 publications

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Mechanism of papain-catalyzed synthesis of oligo-tyrosine peptides

Synthesis of peptides with narrow molecular weight distributions via exopeptidase-catalyzed aminolysis of hydrophobic amino-acid alkyl esters

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