danДоклады Национальной академии наук БеларусиDoklady of the National Academy of Sciences of Belarus1561-83232524-2431The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"dan-444Research ArticleБИОЛОГИЯBIOLOGYСРАВНИТЕЛЬНАЯ КИНЕТИЧЕСКАЯ ХАРАКТЕРИСТИКА РОСТА ШТАММОВ ARTHROBACTER SULFONIVORANS И СИНТЕЗА ВНЕКЛЕТОЧНОЙ БЕТА-ГАЛАКТОЗИДАЗЫCOMPARATIVE KINETIC CHARACTERISTIC OF THE ARTHROBACTER SULFONIVORANS STRAIN GROWTH AND THE EXTRACELLULAR BETA-GALACTOSIDASE SYNTHESISСапуноваЛ. И.SapunovaL. I.

канд. биол. наук, доцент, гл. науч. сотрудник

Ph. D. (Biology), Chief researcher

leonida@mbio.bas-net.byЛобанокА. Г.LobanokA. G.

академик, д-р биол. наук, заведующий лабораторией

Academician, D. Sc. (Biology), Head of the Laboratory

aglobanok@gmail.comТамковичИ. О.TamkovichI. A.

канд. биол. наук, ст. науч. сотрудник

Ph. D. (Biology), Senior researcher

irina-kazakevich@tut.byКостеневичА. А.KastsianevichA. A.

канд. биол. наук, заведующий лабораторией

Ph. D. (Biology), Head of the Laboratory

a.kastsianevich@gmail.comИнститут микробиологии Национальной академии наук БеларусиInstitute of Microbiology of the National Academy of Sciences of Belarus2017051020176148388Copyright © Сапунова Л.И., Лобанок А.Г., Тамкович И.О., Костеневич А.А., 20172017Сапунова Л.И., Лобанок А.Г., Тамкович И.О., Костеневич А.А.Sapunova L.I., Lobanok A.G., Tamkovich I.A., Kastsianevich A.A.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://doklady.belnauka.by/jour/article/view/444

Представлены данные, характеризующие рост исходного БИМ В-2242 и адаптированного к лактозе БИМ В-499-Д штаммов бактерий Arthrobacter sulfonivorans и синтеза ими внеклеточной бета-галактозидазы. Установлено, что адаптированный штамм характеризуется более короткой, чем исходный штамм, лагфазой, раньше достигает максимальной удельной скорости роста (μmax = 0,316–0,319 ч–1) и стационарной фазы развития. Синтез вне-клеточного фермента у обоих штаммов протекает в экспоненциальной фазе роста и достигает одинаковой максимальной удельной скорости (εmax = 0,247–0,250 ед · мг–1 · ч–1) со сдвигом, составляющим 6 ч. При этом штамм БИМ В-499-Д по уровню синтеза фермента в 1,6 раза превосходит штамм БИМ В-2242 при меньшей в 1,3 раза длительности процесса. Кинетические параметры роста (tµmax = 6–9 ч) исследуемых штаммов и образования ими бета-галакто-зидазы (tεmax = 18–24 ч) указывают на разобщенность процессов во времени не менее чем на 12–15 ч.

 

 

 

 

The data are presented on kinetic correlations of the growth of parent and lactose-adapted strains of bacteria Arthrobacter sulfonivorans and the production of extracellular beta-galactosidase. It was found that the adapted strain BIM B-499-D was distinguished by a shorter lag phase than the parent strain BIM B-2242 by a reduced period of reaching a maximum specific growth rate (μmax = 0.316–0.319 h–1) and a stationary phase of culture. Synthesis of extracellular enzyme in both strains occurred during the exponential growth phase and attained a peak specific rate (εmax = 0.247–0.250 U · mg–1 · h–1) with a 6 h time interval. BIM B-499-D exceeds BIM B-22421.6 times in the level of enzyme biosynthesis and in the duration of the process – 1.3 times. The kinetic parameters of growth (tµmax = 6–9 h) and beta-galactosidase production (tεmax = 18–24 h) established for the examined strains indicate the disconnection of processes in time at least by 12–15 h.

 

 

 

 

бактерииArthrobacter sulfonivoransудельная скорость роставнеклеточная бета-галактозидазаудельная скорость синтеза ферментаbacteriaArthrobacter sulfonivoransspecific growth rateextracellular beta-galactosidasespecific rate of enzyme synthesisReferencesHusain, Q. β-Galactosidases and their potential applications: a review / Q. Husain // Crit. Rev. Biotechnol. – 2010. – Vol. 30, N 1. – P. 41–62. doi.org/10.3109/07388550903330497Husain Q. β Galactosidases and their potential applications: a review. Critical Review in Biotechnology, 2010, vol. 30, no. 1, pp. 41–62. doi.org/10.3109/07388550903330497Anisha, G. S. β-Galactosidases / G. S. Anisha // Current Developments in Biotechnology and Bioengineering. Pro duction, Isolation and Purification of Industrial Products / ed. A. Pandey, S. Negi, C. R. Soccol. – Elsevier Publ., 2017. – P. 395–421.Anisha G. S. β-Galactosidases. Pandey A., Negi S., Soccol C. R. (eds.). Current developments in biotechnology and bioengineering. Production, isolation and purification of industrial products, Elsevier Publ., 2017, pp. 395–421.Kastsianevich, A. A. Beta-galactosidases of Arthrobacter bacteria: multiple forms or isoenzymes? / A. A. Kastsianevich, L. I. Sapunova // Научные стремления – 2011: материалы Междунар. науч.-практ. конф. молодых ученых, Минск, 14– 18 ноября 2011 г. – Минск: Белорусская наука, 2011. – Т. 1. – С. 200–206.Kastsianevich A. A., Sapunova L. I. Beta-galactosidases of Arthrobacter bacteria: multiple forms or isoenzymes? Nauchnye stremleniia–2011: materialy mezhdunarodnoi nauchno-practicheskoi konferentsii molodykh uchenykh, Minsk, 14–18 noiabria 2011 goda [Research aspirations–2011: Proceedings of International conference of young scientists, November 14–18, 2011], Minsk: Belorusskaia Nauka Publ., 2011, vol. 1, pp. 200–206 (in Russian).Screening, identification and characterization of Arthrobacter species bacterium producing extracellular beta-galactosidase / A. A. Kastsianevich [et al.] // Труды БГУ, сер. физиол., биохим. и молекул. основы функц. биосистем. – 2014. – Т. 9, Ч. 1. – С. 76–83.Kastsianevich A. A., Sapunova L. I., Bazhanov D. P., Lisov A. V., Leontievsky A. A. Screening, identification and characterization of Arthrobacter species bacterium producing extracellular beta-galactosidase. Trudy Belorusskogo gosudarstvennogo universiteta. Fiziologicheskie, biokhimicheskie i molekuliarnye osnovy funktsionirovaniia biosistem [Works of the Belarussian State University. Physiological, biochemical and molecular bases of functioning of biosystems], 2014, vol. 9, part 1, pp. 76–83 (in Russian).Kuby, S. A. Purification and kinetics of β-galactosidase from E. coli, strain K-12 / S. A. Kuby, H. A. Lardy // J. Amer. Chem. Soc. – 1953. – Vol. 75, N 4. – P. 890–896. doi.org/10.1021/ja01100a035Kuby S. A., Lardy H. A. Purification and kinetics of β-galactosidase from E.coli, strain K-12. Journal of the American Chemical Society, 1953, vol. 75, no. 4, pp. 890–896. doi.org/10.1021/ja01100a035Terui, G. Kinetics of hydrolase production by microorganisms / G. Terui // Pure Appl. Chem. – 1973. – Vol. 56, N 3. – P. 377–395. doi.org/10.1351/pac197336030377Terui G. Kinetics of hydrolase production by microorganisms. Pure and Applied Chemistry, 1973, vol. 56, no. 3, pp. 377– 395. doi.org/10.1351/pac197336030377Остерман, Л. А. Методы исследования белков и нуклеиновых кислот: электрофорез и ультрацентрифугирование / Л. А. Остерман.– М.: Наука, 1981. – C. 66–70.Osterman L. A. Methods of proteins and nucleic acids investigation: Electrophoresis and ultracentrifugation, Moscow, Nauka Publ., 1981, pp. 66–70 (in Russian).Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding / M. M. Bradford // Anal. Biochem. – 1976. – Vol. 72, N 1–2. – P. 248–254. doi. org/10.1016/0003-2697(76)90527-3Bradford M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 1976, vol. 72, no. 1–2, pp. 248–254. doi.org/10.1016/0003-2697(76)90527-3Secreted β-galactosidase from a Flavobacterium sp. isolated from a low-temperature environment / H. P. Sörensen [et al.] // Appl. Microbiol. Biotechnol. – 2006. – Vol. 70, N 5. – P. 548–557. doi.org/10.1007/s00253-005-0153-0Sörensen H. P., Porsgaard T. K., Kahn R. A., Stougaard P., Mortensen K. K., Johnsen M. G. Secreted β-galactosidase from a Flavobacterium sp. isolated from a low-temperature environment. Applied Microbiology and Biotechnology, 2006, vol. 70, no. 5, pp. 548–557. doi.org/10.1007/s00253-005-0153-0Kinetics and metabolism of Bifidobacterium adolescentis MB 239 growing on glucose, galactose, lactose, and galactooligosaccharides / A. Amaretti [et al.] // Appl. Environ. Microbiol. – 2007. – Vol. 73, N 11. – P. 2637–3644. doi. org/10.1128/AEM.02914-06Amaretti A., Bernardi T., Tamburini E., Zanoni S., Lomma M., Matteuzzi D., Rossi M. Kinetics and metabolism of Bifidobacterium adolescentis MB 239 growing on glucose, galactose, lactose, and galactooligosaccharides. Applied and Environmental Microbiology, 2007, vol. 73, no. 11, pp. 2637–2644. doi.org/10.1128/AEM.02914-06Purification and characterization of a novel β-galactosidase from Bacillus sp. MTCC 3088 / S. Chakraborti [et al.] // J. Ind. Microbiol. Biotechnol. – 2000. – Vol. 24, N 1. – P. 58–63. doi.org/10.1038/sj.jim.2900770Chakraborti S., Sani R. K., Banerjee U. C., Sobti R. C. Purification and characterization of a novel β-galactosidase from Bacillus sp. MTCC 3088. Journal of Industrial Microbiology and Biotechnology, 2000, vol. 24, no. 1, pp. 58–63. doi. org/10.1038/sj.jim.2900770Михайлова, Р. В. Мацерирующие ферменты мицелиальных грибов в биотехнологии / Р. В. Михайлова. – Минск: Белорусская наука, 2007. – 407 с.Mikhailova R. V. Macerating enzymes of mycelia fungi in biotechnology. Minsk, Belorusskaia nauka Publ., 2007. 407 p. (in Russian).Мороз, И. В. Кинетические характеристики процессов роста Penicillium piceum F-648 и P. piceum F-648 А3 и синтеза каталаз / И. В. Мороз, Р. В. Михайлова // Молекулярная и прикладная генетика: материалы Междунар. науч. конф., 17–18 нояб. 2005 г. – Минск, 2005. – С. 239.Moroz I. V., Mikhailova R. V. Kinetic characteristics of Penicillium piceum F-648 и P. piceum F-648 А3 growth and catalase synthesis processes. Moleculiarnaia i prikladnaia genetika: materialy mezhdunarodnoi nauchnoi konferentsii, 17–18 noiabria 2005 goda [Molecular and applied genetics: Theses of International scientific conference, November 17–18, 2005]. Minsk, 2005, p. 239. (in Russian).Semashko, T. V. Growth characteristics and glucose oxidase production in mutant Penicillium funiculosum strains / T. V. Semashko, R. V. Mikhailova, A. G. Lobanok // Microbiology (Mikrobiologiya). – 2004. – Vol. 73, N 3. – P. 286–291. doi. org/ 10.1023/B:MICI.0000032238.29220.f7Semashko T. V., Mikhailova R. V., Lobanok A. G. Growth characteristics and glucose oxidase production in mutant Pen-icillium funiculosum strains. Microbiology, 2004, vol. 73, no. 3, pp. 286–291. doi.org/10.1023/B:MICI.0000032238.29220.f7Астапович, Н. И. Некоторые особенности роста Saccharomyces pastorianus и образования полигалактуроназы / Н. И. Астапович, Н. Е. Рябая // Микробиология. – 1996. – Т. 65, № 1. – С. 37–41.Astapovich N. I., Riabaia N. E. Specific features of growth and the biosynthesis of polygalacturonase in Saccharomyces pastorianus. Mikrobiologiya = Microbiology, 1996, vol. 65, no. 1, pp. 37–41 (in Russian).

The authors declare that there are no conflicts of interest present.