OPTIMIZATION OF CULTURE MEDIA FOR AMIDASE CONTAINING BACTERIA

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Published: Oct 29, 2018
Keywords:
amidase activity biomass yield economic coefficient of substrate consumption cultivation

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Юлия/Yuliya Геннадьевна/Gennad'evna Максимова/Maksimova
Institute of Ecology and Genetics of Microorganism UB RAS; Perm State University
Анна/Anna Алексеевна/Alekseevna Гарина/Garina
Perm National Research Polytechnic University
Дмитрий/Dmitry Михайлович/Mikhailovich Васильев/Vasilyev
Institute of Ecology and Genetics of Microorganism UB RAS
Александр/Aleksandr Юрьевич/Yur'evich Максимов/Maksimov
Institute of Ecology and Genetics of Microorganism UB RAS; Perm State University

Abstract

The growth characteristics of Gram-negative amidase containing bacteria of Acinetobacter guillouiae llh, Pseudomonas monteilii 5, Alcaligenes faecalis 2 under cultivation in the medium with different concentrations of glucose, sucrose, acetamide and sodium acetate as a carbon were studied. The aim of the work was to optimize the synthetic mineral medium by the source of carbon. It has been determined that the best growth substrate for the manifestation of the amidase activity of the strains was acetamide. With a combination of characteristics such as the biomass yield, the economic coefficient of substrate consumption and enzymatic activity, the optimal acetamide concentration for A. guillouiae llh was 0.025 M, for A faecalis 2 - 0.l M. The growth dynamics of A. faecalis 2 on acetamide in different concentrations was studied. It was shown that the 0.025 M acetamide was insufficient for intensive growth of bacteria, and 0.5 M was inhibitory.

Article Details

How to Cite
Максимова/Maksimova Ю. Г., Гарина/Garina А. А., Васильев/Vasilyev Д. М., & Максимов/Maksimov А. Ю. (2018). OPTIMIZATION OF CULTURE MEDIA FOR AMIDASE CONTAINING BACTERIA. Bulletin of Perm University. Biology, (2), 193–199. Retrieved from https://press.psu.ru/index.php/bio/article/view/1853
Issue
No. 2 (2017): Вестник Пермского университета. Серия «Биология»=Bulletin of Perm University. Biology
Section
Микробиология

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Author Biographies

Юлия/Yuliya Геннадьевна/Gennad'evna Максимова/Maksimova, Institute of Ecology and Genetics of Microorganism UB RAS; Perm State University

Doctor of biology, Leading Researcher of the Laboratory of Molecular Microbiology and Biotechnology;Associate professor of the Department of Microbiology and Immunology

Анна/Anna Алексеевна/Alekseevna Гарина/Garina, Perm National Research Polytechnic University

Student

Дмитрий/Dmitry Михайлович/Mikhailovich Васильев/Vasilyev, Institute of Ecology and Genetics of Microorganism UB RAS

Candidate of biology, junior scientist of the laboratory of molecular microbiology and biotechnology

Александр/Aleksandr Юрьевич/Yur'evich Максимов/Maksimov, Institute of Ecology and Genetics of Microorganism UB RAS; Perm State University

Candidate of biology, senior scientist of the laboratory of molecular microbiology and biotechnology;Associate professor of the Department of Microbiology and Immunology

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Fournand D., Bigey F., Arnaud A. Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic acids. Applied and Environmental Microbiology, V. 64 (1998): pp. 2844-2852.

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Jebasingh S.E.J. et al. Biodegradation of acrylamide and purification of acrylamidase from newly isolated bacterium Moraxella osloensis MSU11. International Biodeterioration & Biodegradation, V. 85 (2013): pp. 120-125.

Jin L.-Q. et al. Efficient biocatalytic hydrolysis of 2-chloronicotinamide for production of 2-chloronicotinic acid by recombinant amidase. Catalysis Communications, V. 38 (2013): pp. 6-9.

Mehta P.K. et al. Thermostable amidase catalyzed production of isonicotinic acid from isonicotina-mide. Process Biochemistry, V. 50 (2015): pp. 1400-1404.

Mehta P.K. et al. Enhanced production of thermostable amidase from Geobacillus subterraneus RL-2a MTCC 11502 via optimization of physicochemi-cal parameters using Taguchi DOE methodology. 3 Biotech., V. 6 (2016): pp. 66.

Nojiri M., Taoka N., Yasohara Y. Characterization of an enantioselective amidase from Cupriavidus sp. KNK-J915 (FERM BP-10739) useful for enzymatic resolution of racemic 3-piperidinecarboxamide. Journal of Molecular Catalysis B: Enzymatic, V. 109 (2014): pp. 136-142.

Prasad S., Sharma D.R., Bhalla T.C. Nitrile- and amide hydrolysing activity in Kluyveromyces thermo-tolerans MGBY 37. World Journal of Microbiology and Biotechnology, V. 21, (2005): pp. 14471450.

Ruan L.-T. et al. Purification and characterization of R-stereospecific amidase from Brevibacterium epider-midis ZJB-07021. International Journal of Biological Macromolecules, V. 86 (2016): pp. 893-900.

Sharma M., Sharma N.N., Bhalla T.C. Amidases: versatile enzymes in nature. Reviews in Environmental Science and Bio/Technology, V. 8 (2009): pp. 343-366.

Wu Z.-M., Zheng R.-C., Zheng Y.-G. Exploitation and characterization of three versatile amidase su-perfamily members from Delftia tsuruhatensis ZJB-05174. Enzyme and Microbial Technology, V. 86 (2016): pp. 93-102.

Wu Z.-M., Zheng R.-C., Zheng Y.-G. Identification and characterization of a novel amidase signature family amidase from Parvibaculum lavamen-tivorans ZJB14001. Protein Expression and Purification, V. 129 (2017): pp. 60-68.

Zheng R.-C. et al. Industrial production of chiral intermediate of cilastatin by nitrile hydratase and amidase catalyzed one-pot, two-step biotransformation. Journal of Molecular Catalysis B: Enzymatic, V. 102 (2014): pp. 161-166.

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