Nucleolytic enzymes from the marine bacterium Cobetia amphilecti KMM 296 with antibiofilm activity and biopreservative effect on meat products

Balabanova, Larissa; Podvolotskaya, Anna; Slepchenko, Lubov; Елисейкина, М. Г.; Noskova, Yulia; Nedashkovskaya, Olga I.; Son, Oksana; Tekutyeva, Liudmila; Rasskazov, V. A.

doi:10.1016/j.foodcont.2017.02.029

Cited by 19 publications

(30 citation statements)

References 26 publications

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“…The alkaline phosphatase CmAP from C. amphilecti KMM 296 was also shown to effectively inhibit the growth of the new biofilms and degradation of the mature biofilms of S. enteritidis, as well as P. aeruginosa and B. subtilis [7], in contrast to CamPhoD. The antibacterial activity of the alkaline phosphatase against P. aeruginosa has been found in E. coli, which is known as a causative agent of diarrhea [58].…”

Section: Effect Of Camphod On Bacterial Biofilmsmentioning

confidence: 99%

“…The presence of extracellular alkaline phosphatases of the structural families PhoA (GenBank ID: WP_084589490.1) and PhoD (GenBank ID: WP_043333989.1) in the marine gamma-proteobacterium C. amphilecti KMM 296 may indicate either their distinct or cooperative functions for the hydrolysis of various phosphorus-containing organic molecules, depending on the environmental conditions and cell lifestyle [7,36]. The analogous PhoD enzyme from B. subtilis is thought to target specific phosphate-containing molecules, such as teichoic acids linked to the wall peptidoglycan via phosphodiester bonds.…”

Section: Effect Of Camphod On Bacterial Biofilmsmentioning

confidence: 99%

“…The PhoA alkaline phosphatase (CmAP) of the marine bacterium C. amphilecti KMM 296 (Collection of Marine Microorganisms, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, the Russian Academy of Sciences (PIBOC FEB RAS)) isolated from the coelomic fluid of the mussel, Crenomytilus grayanus, was suggested to promote the host mollusk shell's mineralization and biofilm regulation of many species of food-derived pathogens [6,7,12]. The mechanism of the CmAP biological action is still unclear and remains under investigation.…”

Section: Introductionmentioning

confidence: 99%

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A Novel Alkaline Phosphatase/Phosphodiesterase, CamPhoD, from Marine Bacterium Cobetia amphilecti KMM 296

et al. 2019

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A novel extracellular alkaline phosphatase/phosphodiesterase from the structural protein family PhoD that encoded by the genome sequence of the marine bacterium Cobetia amphilecti KMM 296 (CamPhoD) has been expressed in Escherichia coli cells. The calculated molecular weight, the number of amino acids, and the isoelectric point (pI) of the mature protein’s subunit are equal to 54832.98 Da, 492, and 5.08, respectively. The salt-tolerant, bimetal-dependent enzyme CamPhoD has a molecular weight of approximately 110 kDa in its native state. CamPhoD is activated by Co2+, Mg2+, Ca2+, or Fe3+ at a concentration of 2 mM and exhibits maximum activity in the presence of both Co2+ and Fe3+ ions in the incubation medium at pH 9.2. The exogenous ions, such as Zn2+, Cu2+, and Mn2+, as well as chelating agents EDTA and EGTA, do not have an appreciable effect on the CamPhoD activity. The temperature optimum for the CamPhoD activity is 45 °C. The enzyme catalyzes the cleavage of phosphate mono- and diester bonds in nucleotides, releasing inorganic phosphorus from p-nitrophenyl phosphate (pNPP) and guanosine 5′-triphosphate (GTP), as determined by the Chen method, with rate approximately 150- and 250-fold higher than those of bis-pNPP and 5′-pNP-TMP, respectively. The Michaelis–Menten constant (Km), Vmax, and efficiency (kcat/Km) of CamPhoD were 4.2 mM, 0.203 mM/min, and 7988.6 S−1/mM; and 6.71 mM, 0.023 mM/min, and 1133.0 S−1/mM for pNPP and bis-pNPP as the chromogenic substrates, respectively. Among the 3D structures currently available, in this study we found only the low identical structure of the Bacillus subtilis enzyme as a homologous template for modeling CamPhoD, with a new architecture of the phosphatase active site containing Fe3+ and two Ca2+ ions. It is evident that the marine bacterial phosphatase/phosphidiesterase CamPhoD is a new structural member of the PhoD family.

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Section: Effect Of Camphod On Bacterial Biofilmsmentioning

confidence: 99%

Section: Effect Of Camphod On Bacterial Biofilmsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Novel Alkaline Phosphatase/Phosphodiesterase, CamPhoD, from Marine Bacterium Cobetia amphilecti KMM 296

et al. 2019

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“…In the marine bacteria Cobetia amphilecti KMM 296 and Pseudoalteromonas sp. KMM 701, candidates for the active metabolites may be hydrolytic enzymes [ 3 , 4 ]. When applying the highly active alkaline phosphatase CmAP from C. amphilecti KMM 296 or α-galactosidase α-PsGal from Pseudoalteromonas sp.…”

Section: Introductionmentioning

confidence: 99%

“…KMM 701 on the mature biofilms of P. aeruginosa , Salmonella enteritidis , Staphylococcus aureus , and Bacillus subtilis isolated from the frozen ready-to-cook meat, a visible effect of their degradation was observed after a few hours of the enzymatic treatment [ 5 ]. The effect might be caused by the quorum sensing (QS)-mediated switching from the high to low (or contrarily) level of the biofilm-associated gene expression under the growth of bacterial cultures with the addition of the enzymes, or under the enzymatic treatment of their mature biofilms [ 3 ]. There are many studies focused on the strategy to inhibit or accelerate the bacterial cells’ physiological processes through disrupting or modulating their QS [ 2 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Genomic Features of a Food-Derived Pseudomonas aeruginosa Strain PAEM and Biofilm-Associated Gene Expression under a Marine Bacterial α-Galactosidase

Balabanova

Shkryl

Slepchenko

et al. 2020

IJMS

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The biofilm-producing strains of P. aeruginosa colonize various surfaces, including food products and industry equipment that can cause serious human and animal health problems. The biofilms enable microorganisms to evolve the resistance to antibiotics and disinfectants. Analysis of the P. aeruginosa strain (serotype O6, sequence type 2502), isolated from an environment of meat processing (PAEM) during a ready-to-cook product storage (−20 °C), showed both the mosaic similarity and differences between free-living and clinical strains by their coding DNA sequences. Therefore, a cold shock protein (CspA) has been suggested for consideration of the evolution probability of the cold-adapted P. aeruginosa strains. In addition, the study of the action of cold-active enzymes from marine bacteria against the food-derived pathogen could contribute to the methods for controlling P. aeruginosa biofilms. The genes responsible for bacterial biofilm regulation are predominantly controlled by quorum sensing, and they directly or indirectly participate in the synthesis of extracellular polysaccharides, which are the main element of the intercellular matrix. The levels of expression for 14 biofilm-associated genes of the food-derived P. aeruginosa strain PAEM in the presence of different concentrations of the glycoside hydrolase of family 36, α-galactosidase α-PsGal, from the marine bacterium Pseudoalteromonas sp. KMM 701 were determined. The real-time PCR data clustered these genes into five groups according to the pattern of positive or negative regulation of their expression in response to the action of α-galactosidase. The results revealed a dose-dependent mechanism of the enzymatic effect on the PAEM biofilm synthesis and dispersal genes.

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Cobetia

Ventosa¹,

Arahal²

2020

Bergey's Manual of Systematics of Archaea and Bacteria

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Co.be′ti.a. N.L. fem. n. Cobetia named after A. B. Cobet, who originally described the type species as “ Arthrobacter marinus .” Proteobacteria / Gammaproteobacteria / Oceanospirillales / Halomonadaceae / Cobetia The genus Cobetia is classified within the family Halomonadaceae and the order Oceanospirillales , in the class Gammaproteobacteria . The cells stain Gram‐negative and are motile and non‐endospore‐forming rods. Colonies are cream, white, or light yellow pigmented. Chemoorganotrophic. Strictly aerobic. Catalase‐positive and oxidase‐negative. Optimal growth at 5–6.5% (w/v) NaCl, at pH 6.5–8.5 and 25–38°C. The predominant cellular fatty acids are C 16:1 ω7 c , C 16:0 , C 12:0 3‐OH, C 18:1 ω7 c , and C 17:0 cyclo. The DNA G + C content is 61.4–64.6 mol%. Currently, the genus includes five species: Cobetia marina (type species of the genus), Cobetia amphilecti , Cobetia crustatorum , Cobetia litoralis, and Cobetia pacifica . The strains of these species were isolated from marine environments, marine sediments, marine invertebrates, and fermented seafood. DNA G + C content (mol%): 61.4–64.6 according to wet‐lab methods, 57.3–63.2 in genomic sequences. Type species: Cobetia marina (Cobet et al. 1970) Arahal et al. 2002a VL88, emend. Romanenko et al. 2013.

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Nucleolytic enzymes from the marine bacterium Cobetia amphilecti KMM 296 with antibiofilm activity and biopreservative effect on meat products

Cited by 19 publications

References 26 publications

A Novel Alkaline Phosphatase/Phosphodiesterase, CamPhoD, from Marine Bacterium Cobetia amphilecti KMM 296

A Novel Alkaline Phosphatase/Phosphodiesterase, CamPhoD, from Marine Bacterium Cobetia amphilecti KMM 296

Genomic Features of a Food-Derived Pseudomonas aeruginosa Strain PAEM and Biofilm-Associated Gene Expression under a Marine Bacterial α-Galactosidase

Cobetia

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