Mikrobiol. Z. 2019; 81(3):14-26. Russian.
Glycosidase Activity of Bacteria the Genus Bacillus, Isolated from the Black Sea
Gudzenko E.V.1, Borzova N.V.1, Varbanets L.D.1, Ivanitsa V.A.2, Seifullina I.I.2,
Martsinko E.E.2, Pirozhok O.V.2, Chebanenko E.A.2
1Zabolotny Institute of Microbiology and Virology, NAS of Ukraine
154 Akad. Zabolotny Str., Kyiv, 03143, Ukraine
2Odesa Mechnikov National University
2 Dvoryanskaya Str., Odesa, 65082, Ukraine
High biotechnology potential of marine microorganisms as producers of enzymes has been driving extensive research of their diversity and biological features in recent years, including the active screening of glycosidases of marine bacteria for commercial applications. The aim of this paper was to study the ability of bacteria isolated from the bottom sediments of the Black Sea to produce glycosidases of various specificities, as well as to investigate the possibility of using coordination compounds of germanium to increase the enzymatic activity of bacteria of the genus Bacillus. Methods. The cultivation of bacteria was carried out in submerged conditions; maltose and rhamnose were used as carbon sources. Glycosidases activities were determined by the Romero and Davis method, protein - by the Lowry method. Coordination compounds of germanium were used as effectors of biosynthesis and activity of α-L-rhamnosidase in concentrations of 0.1 and 0.01%. Results. Based on the screening of 12 glycosidases activities (β-D-galactosidase, β-D-glucuronidase, α-D-mannosidase, α-D-xylosidase, α-D-fucosidase, β-D-xylosidase, β-D-glucosidase, N-acetyl-β-D-glucosaminidase, N-acetyl-α-D-glucosaminidase, N-acetyl-β-D-galactosaminidase, α-D-glucosidase, α-L-rhamnosidase) among 10 cultures of Bacillus, α-L-rhamnosidase activity (0.03-0.18 U/mg protein) was detected in 8 strains. Culture of Bacillus sp. 19 was the most active. Decrease in α-L-rhamnosidase activity of a Bacillus sp. 19 was observed after introduction of germanium complexes (0.1 and 0.01%) into the growth medium. We showed that bis (bipyridine) chloromodynam (II) bis (citrato) germanate (IV) octahydrate and tris (bipyridine) nickel (II) bis (citrato) germanate(IV) monohydrate can be used to increase α-L-rhamnosidase activity of Bacillus sp. 19. Conclusions. α-L-Rhamnosidase activity of marine strains belonging to the species of Bacillus licheniformis, Bacillus atrophaus, Bacillus subtiliswas shown for the first time. Activation of α-L-rhamnosidase from Bacillus sp. 19 by coordination compounds of germanium was observed.
Keywords: glycosidase, α-L-rhamnosidase activity, bacteria of the Black Sea, Bacillus, screening, coordination compounds of germanium.
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- Murphy BT, Jensen PR, Fenical W. The chemistry of marine bacteria. In: Fattorusso E., Gerwick W., Taglialatela-Scafati O., eds. Handbook of Marine Natural Products. Springer, Dordrecht. 2012; 153-190. https://doi.org/10.1007/978-90-481-3834-0_3
- Joint I, Mühling M, Querellou J. Culturing marine bacteria - an essential prerequisite for biodiscovery. Microb Biotechnol. 2010; 3(5):564-575. https://doi.org/10.1111/j.1751-7915.2010.00188.x
- Schinke C, Martins T. Antibacterial compounds from marine bacteria, 2010-2015. J Nat Prod. 2017; 80(4):1215-1228. https://doi.org/10.1021/acs.jnatprod.6b00235
- Paulsen SS, Andersen B, Gram L, Machado H. Biological potential of chitinolytic marine bacteria. Marine Drugs. 2016; 14(12):230. https://doi.org/10.3390/md14120230
- Kalitnik AA, Nedashkovskaya OI, Stenkova AM. Carrageenanolytic enzymes from marine bacteria associated with the red alga Tichocarpus crinitus. J Appl Phycol. 2017; 30(1):1-11. https://doi.org/10.1007/s10811-017-1355-4
- El-Hassayeb AEH, Abdel-Aziz ZMS. Screening, production and industrial application of protease enzyme from marine bacteria. Int J Curr Microbiol App Sci. 2016; 5(7):863-874. https://doi.org/10.20546/ijcmas.2016.507.099
- Bakunina IYu, Nedashkovskaya OI, Kim SB, Zvyagintseva TN, Mikhhailov VV. Diversity of glycosidase activities in the bacteria of the phylum Bacteroidetes isolated from marine algae. Microbiologia. 2012; 81(6):155-160. https://doi.org/10.1134/S0026261712060033
- Michel G, Czjzek M. Polysaccharide-degrading enzymes from marine bacteria. In book: Marine enzymes for biocatalysis: sources, biocatalytic characteristics and bioprocesses of marine enzymes. Publisher: Wood head Publishing Limited Eds: Trincone A. 2013: 429-464. https://doi.org/10.1533/9781908818355.3.429
- Izzo V, Tedesco P, Notomista E, Pagnotta E, Di Donato A, Trincone A, Tramice A. α-Rhamnosidase activity in the marine isolate Novosphingobium sp. PP1Y and its use in the bioconversion of flavonoids. J Mol Catal B Enzym. 2014; 105: 95-103. https://doi.org/10.1016/j.molcatb.2014.04.002
- Nakamura T, Shimada Y, Takeda T, Sato K, Akiba M, Fukaya H. Organogermanium compound, Ge-132, forms complexes with adrenaline, ATP and other physiological cis-diol compounds. Future Med Chem. 2015;7(10):1233-1246. https://doi.org/10.4155/fmc.15.62
- Tezuka T, Higashino A, Akiba M, Nakamura T. Organogermanium (Ge-132) suppresses activities of stress enzymes responsible for active oxygen species in monkey liver preparation. AER. 2017; 5(2):13-23. https://doi.org/10.4236/aer.2017.52002
- Ali MM, Noaman E, Kamal Sh, Soliman S, Ismail DA. Role of germanium L-cysteine α-tocopherol complex as stimulator of some antioxidant defense systems in gammairradiated rats. Acta Pharm. 2007; 57:1-12. https://doi.org/10.2478/v10007-007-0001-0
- Lepikh YaI, Smyntyna VA, Snigur PO, Olikh YaM. Germanium coordination compounds - structure, properties, possible applications. J Physics: Conference Series. 2007; 76(1):012050. https://doi.org/10.1088/1742-6596/76/1/012050
- Romero C, Manjon A, Bastida J. A method for assaying rhamnosidase activity of naringinase. Anal Biochem. 1985; 149(2):566-571. https://doi.org/10.1016/0003-2697(85)90614-1
- Davis DW. Determination of flavonones in citrus juice. Anal Biochem. 1947; 19(1):46-48. https://doi.org/10.1021/ac60007a016
- Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with folin phenol reagent. J Biol Chem. 1951; 193(2):265-275.
- Orrillo AG, Ledesma P, Delgado OD, Spagna G, Breccia JD. Cold-active α-Lrhamnosidase from psychrotolerant bacteria isolated from a sub-Antarctic ecosystem. Enzyme Microb Technol. 2007; 40:236-241. https://doi.org/10.1016/j.enzmictec.2006.04.002
- Yadav P, Chauhan AK, Singh PS. α-L-Rhamnosidase: sources, production, purification and characterization of the debittering enzyme. IJBTR.2017; 7(1):1-10.
- Alvarenga AE, Romero CM, Castro GR. A novel α-L-rhamnosidase with potential applications in citrus juice industry and in winemaking. Eur Food Res Technol. 2013; 237(6):977-985. https://doi.org/10.1007/s00217-013-2074-y
- Shubchyns'ka AS, Varbanets LD., Seĭfullina II., Martsynko OE, Piesarohlo OH. [Effect of coordination germanium compounds on biosynthesis and activity of proteases in Bacillus sp. and Yarrowia lipolytica]. Mikrobiol Z. 2008; 70(4):3-9. Ukrainian.