Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli

García-Fraga, Belén; Silva, Abigail F. da; López-Seijas, Jacobo; Sieiro, Carmen

doi:10.1007/s00253-013-5124-2

Cited by 37 publications

(32 citation statements)

References 31 publications

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“…When KOH was chosen as the neutralizing agent, a maximum cell growth of 1.02 g/l and a maximum chitinase activity of 10.0 U/ml was achieved, which were a little greater than in the case of NaOH. These results suggest that K + promotes chitinase activity, as has been reported for the chitinase of Halobacterium salinarum (Garcia-Fraga et al, 2014). Thus, more GlcNAc was produced by the hydrolysis of chitin and made available for cell growth and more chitinase was accumulated.…”

Section: Effect Of Different Neutralizing Agentssupporting

confidence: 61%

Enhanced chitinase production by <i>Chitinolyticbacter meiyuanensis</i> SYBC-H1 using staged pH control

Zhang

Gao

Chen

et al. 2016

J. Gen. Appl. Microbiol.

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None of the authors of this manuscript has any financial or personal relationship with other people or organizations that could inappropriately influence their work.to their wide range of biotechnological applications, such as shellfish waste management (Nakagawa et al., 2011), generation of fungal protoplasts (Fleuri et al., 2009), production of single cell protein (Wang et al., 2006), production of N-acetyl-b-D-glucosamine (GlcNAc) and derivatives (Lin et al., 2009) and bio-control of fungal plant pathogens (Joo, 2005).Despite the potential commercial benefits, the application of chitinases has been limited by low productivity (Liu et al., 2013), which is of particular relevance to the production by the enzymatic degradation of chitin. Thus, increasing the levels of chitinase production is a key to improving GlcNAc production on an industrial scale. In a previous study, increasing the chitinase production , mainly via strain screening (Meena et al., 2013), strain mutation (Li et al., 2007), genetic modification (Iqbal et al., 2012) and medium optimization (Singh et al., 2013). Furthermore, the control of culture conditions, including the pH, was shown to be important for controlling the level of chitinase activity.The effect of pH on cell growth and enzyme production differs among microorganisms. Chitinase can be divided into alkaline (Bhushan and Hoondal, 1998), acidic (Chang et al., 2014), and neutral (Takeo et al., 2009) chitinase, according to its isoelectric point. The change of the growth medium pH owing to the accumulation of GlcNAc produced by the hydrolysis of chitin (Halder et al., 2013) does not benefit both cell growth and chitinase production in chitinase fermentation. However, there are few reports about the effect of pH on chitinase production in batch fermentation.A highly efficient chitinolytic bacterium Chitinolyticbacter meiyuanensis SYBC-H1 producing alkaline chitinase was isolated in our lab (Hao et al., 2011a, b;Zhang et al., 2016). In the present study, the influence Enhanced chitinase production by Chitinolyticbacter meiyuanensis SYBC-H1 using staged pH control (Received August 22, 2015 The pH of a microbiological culture is important for both cell growth and chitinase accumulation, but the optimal pH is not normally the same for both. The objective of this study was to investigate the effect of pH on chitinase production by Chitinolyticbacter meiyuanensis strain SYBC-H1 (ATCC BAA-2140) in a mineral medium. The results of batch culture at different pH values showed that the optimum pH for cell growth and chitinase production varied with time, although KOH produced the best results for cell growth and chitinase production, NaOH was chosen because of cost considerations. We designed a three-stage pH control strategy using NaOH as the neutralizing agent. Maximum cell growth (1.07 g dry cell weight/l) and maximum chitinase activity (13.6 U/ml) were observed after culture at 26∞C for 72 h in a mineral medium. These values were greater by 129% and 162%, respectively, and the length of time...

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Section: Effect Of Different Neutralizing Agentssupporting

confidence: 61%

Enhanced chitinase production by <i>Chitinolyticbacter meiyuanensis</i> SYBC-H1 using staged pH control

Zhang

Gao

Chen

et al. 2016

J. Gen. Appl. Microbiol.

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“…So far, many microbial chitinases have been identified and characterized [1,12,13], whereas there is still few information on the chitinases from marine bacteria [10,11,14,15]. Two chitinases from marine bacterium Paenibacillus barengoltzii have been reported in our recent studies: PbChi70 is an endo type chitinase with a molecular mass of 70.6 kDa.…”

Section: Discussionmentioning

confidence: 97%

“…They have been considered as excellent sources of chitinases, and some chitinases have been isolated from marine bacteria, such as Halobacterium salinarum [15], Pseudoalteromonas sp. [16] and Pseudoaltermonas tunicata [14].…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Yan

Wang

et al. 2016

International Journal of Biological Macromolecules

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“…salinarum CECT 395 was cloned and overexpressed as a 66.5 kDa protein in E. coli. The purified recombinant chitinase displayed optimum activity at pH 7.3 and 40 C, with high stability over broad pH (6-8.5) and temperature C) ranges [259].…”

Section: Cellulasesmentioning

confidence: 99%

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

et al. 2017

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Halophilic archaea, also referred to as haloarchaea, dominate hypersaline environments. To survive under such extreme conditions, haloarchaea and their enzymes have evolved to function optimally in environments with high salt concentrations and, sometimes, with extreme pH and temperatures. These features make haloarchaea attractive sources of a wide variety of biotechnological products, such as hydrolytic enzymes, with numerous potential applications in biotechnology. The unique trait of haloarchaeal enzymes, haloenzymes, to sustain activity under hypersaline conditions has extended the range of already-available biocatalysts and industrial processes in which high salt concentrations inhibit the activity of regular enzymes. In addition to their halostable properties, haloenzymes can also withstand other conditions such as extreme pH and temperature. In spite of these benefits, the industrial potential of these natural catalysts remains largely unexplored, with only a few characterized extracellular hydrolases. Because of the applied impact of haloarchaea and their specific ability to live in the presence of high salt concentrations, studies on their systematics have intensified in recent years, identifying many new genera and species. This review summarizes the current status of the haloarchaeal genera and species, and discusses the properties of haloenzymes and their potential industrial applications. SYSTEMATICS OF HALOPHILIC ARCHAEAHalophilic micro-organisms are found in the three domains of life, and are extremophiles living in hypersaline environments in the presence of salt (generally NaCl) as a specific requisite for their growth [1]. Hypersaline environments contain higher salt concentrations than seawater (3.5 % total dissolved salts) [2]. According to the optimum NaCl concentration for growth, micro-organisms fall into one of the following categories: extreme halophiles with optimum growth at 15-30 % (2.5-5.2 M) NaCl; moderate halophiles with optimum growth at 3-15 % (0.5-2.5 M) NaCl; slight halophiles with optimum growth at 1-3 % (0.2-0.5 M) NaCl; non-halophiles with optimum growth at less than 1 % (0.2 M) NaCl; and halotolerant micro-organisms which are non-halophiles showing the ability to tolerate high NaCl concentrations [3]. Halophiles can live in hypersaline environments because they are able to sustain osmotic balance. They use two main strategies to withstand the adverse consequences of water loss when exposed to high salt concentrations. The first strategy used by extremely halophilic archaea (haloarchaea) and halophilic anaerobic bacteria such as members of Halanaerobiales is known as the 'salt-in-cytoplasm' strategy, during which salts such as NaCl or KCl accumulate in the cytoplasm at concentrations similar to the extracellular ones [4,5]. Another mechanism to cope with high salt concentrations is the accumulation of organic molecules such as amino acids, sugars and polyols, known as compatible solutes or osmolytes. Compatible solutes are small and highly soluble molecules that can...

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Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli

Cited by 37 publications

References 31 publications

Enhanced chitinase production by <i>Chitinolyticbacter meiyuanensis</i> SYBC-H1 using staged pH control

Enhanced chitinase production by <i>Chitinolyticbacter meiyuanensis</i> SYBC-H1 using staged pH control

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

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