Resolution of non-protein amino acids via the enantioselective hydrolysis of their esters mediated by sulfhydryl proteases

1994 ◽  
Vol 16 (4) ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Hitoshi Iwanaga ◽  
Takashi Yamada ◽  
Shigeru Kuwata
Tetrahedron ◽  
2005 ◽  
Vol 61 (43) ◽  
pp. 10254-10261 ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Kiwamu Imagawa ◽  
Hiroe Minowa ◽  
Toyoko Miyamoto ◽  
Takashi Yamada

ACS Catalysis ◽  
2011 ◽  
Vol 1 (9) ◽  
pp. 1014-1016 ◽  
Author(s):  
Maeve O’Neill ◽  
Bernhard Hauer ◽  
Nina Schneider ◽  
Nicholas J. Turner

1989 ◽  
Vol 18 (12) ◽  
pp. 2219-2222 ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Hitoshi Iwanaga ◽  
Shinichi Ueji ◽  
Takashi Yamada ◽  
Shigeru Kuwata

2021 ◽  
Vol 37 (5) ◽  
pp. 41-48
Author(s):  
P.Yu. Tadzhibova ◽  
N.I. Ignatova ◽  
M.B. Overchenko ◽  
N.S. Pogorzhelskaya ◽  
L.V. Rimareva

Abstract-The preparation of fermented sauces by the conversion of soy raw materials under the action of the A. oryzae RCAM 01134 fungus or endogenous enzymes is described. The technologies differed at the first stage of fermentation: the fungus development lasted for 4 days, and the hydrolysis of soy polymers under the action of a selected enzyme complex continued for 24 h. An algorithm was developed for the process of biocatalytic conversion of soy polymers using enzymes of various mechanisms of action and origin. Soy proteins were hydrolyzed most effectively by a complex enzyme preparation containing proteinases, peptidases, xylanases and α-amylases. It provided the level of formation of amine nitrogen and free amino acids in the enzymatic hydrolysate by 3.6-3.8 times higher than the autolytic conversion. The specific influence of biotechnological methods on the composition of the obtained fermented soy sauces was revealed. Microbial conversion contributed to an increase in the content of essential amino acids in the products (by 1.72 times) and a decrease in the level of carbohydrates (by 1.7 times), while enzymatic hydrolysis was characterized by a higher release of amino acids from the bound state (53.8 %). Key words: soybeans, bioconversion, Aspergillus oryzae, enzymes, proteases, xylanase, α-amylase, fermented sauce, protein, amino acids The work was carried out at the expense of subsidies for the implementation of a state task (topic no. 0529-2019-0066).


MRS Advances ◽  
2020 ◽  
Vol 5 (52-53) ◽  
pp. 2669-2678
Author(s):  
Jeovani González P. ◽  
Ramiro Escudero G

AbstractDeinking of recycled office (MOW) paper was carried out by using a flotation column and adding separately sodium hydroxide, and the enzyme Cellulase Thricodema Sp., as defibrillators.The de-inked cellulose fibers were characterized according to the standards of the paper industry, to compare the efficiency of the deinking of each chemical reagent used to hydrolyze the fibers and defibrillate them.The computational simulation of the molecular coupling between the enzyme and cellulose was performed, to establish the enzyme-cellulose molecular complex and then to identify the principal amino-acids of endo-β-1,4-D-glucanase in this molecular link, which are responsible for the hydrolysis of the cellulose.Experimental results show the feasibility to replace sodium hydroxide with the enzyme Cellulase Thricodema Sp., by obtaining deinked cellulose with similar optical and physical properties.The use of the enzyme instead of sodium hydroxide avoids the contamination of the residual water; in addition to that, the column is operated more easily, taking into consideration that the pH of the system goes from alkaline to neutral.


2018 ◽  
Vol 69 (10) ◽  
pp. 2794-2798
Author(s):  
Alina Diana Panainte ◽  
Ionela Daniela Morariu ◽  
Nela Bibire ◽  
Madalina Vieriu ◽  
Gladiola Tantaru ◽  
...  

A peptidic hydrolysate has been obtained through hydrolysis of bovine hemoglobin using pepsin. The fractioning of the hydrolysate was performed on a column packed with CM-Sepharose Fast Flow. The hydrolysate and each fraction was filtered and then injected into a HPLC system equipped with a Vydak C4 reverse phase column (0.46 x 25 cm), suitable for the chromatographic separation of large peptides with 20 to 30 amino acids. The detection was done using mass spectrometry, and the retention time, size and distribution of the peptides were determined.


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