Enhanced production of protease by <i>Pseudoalteromonas arctica</i> PAMC 21717 via statistical optimization of mineral components and fed-batch fermentation

Han, Se Jong; Park, Heeyong; Kim, Sunghui; Kim, Dockyu; Park, Ha Ju; Yim, Joung Han

doi:10.1080/10826068.2015.1031390

Cited by 11 publications

(10 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Extracellular serine proteases, metalloproteases, and other less-characterized proteolytic substances are also produced by some Pseudoalteromonas spp. (8,(11)(12)(13)(14)(15)(16)(17) and are, in most cases, believed to serve as antibacterial agents or to remove proteinaceous material from biofilms (18,19). It has been suggested that Pseudoalteromonas and other bacteria that are associated with the surface of corals produce antimicrobial compounds that may serve as a mechanism to protect corals from pathogens (20,21), although Choudhury et al (15) reported on a strain of Pseudoalteromonas agarivorans that was a sponge pathogen.…”

mentioning

confidence: 99%

Mechanisms for Pseudoalteromonas piscicida-Induced Killing of Vibrios and Other Bacterial Pathogens

Richards

Watson

Needleman

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

is a Gram-negative gammaproteobacterium found in the marine environment. Three strains of pigmented were isolated from seawater and partially characterized by inhibition studies, electron microscopy, and analysis for proteolytic enzymes. Growth inhibition and death occurred around colonies of on lawns of the naturally occurring marine pathogens ,, ,, and Inhibition also occurred on lawns of but not on O157:H7 or serovar Typhimurium. Inhibition was not pH associated, but it may have been related to the secretion of a cysteine protease with strong activity, as detected with a synthetic fluorogenic substrate. This diffusible enzyme was secreted from all three strains. Direct overlay of the colonies with synthetic fluorogenic substrates demonstrated the activity of two aminopeptidase Bs, a trypsin-like serine protease, and enzymes reactive against substrates for cathepsin G-like and caspase 1-like proteases. In seawater cultures, scanning electron microscopy revealed numerous vesicles tethered to the outer surface of and a novel mechanism of direct transfer of these vesicles to Vesicles digested holes in cells, while the congregated around the vibrios in a predatory fashion. This transfer of vesicles and vesicle-associated digestion of holes were not observed in other bacteria, suggesting that vesicle binding may be mediated by host-specific receptors. In conclusion, we show two mechanisms by which inhibits and/or kills competing bacteria, involving the secretion of antimicrobial substances and the direct transfer of digestive vesicles to competing bacteria. species are widespread in nature and reduce competing microflora by the production of antimicrobial compounds. We isolated three strains of and characterized secreted and cell-associated proteolytic enzymes, which may have antimicrobial properties. We identified a second method by which kills It involves the direct transfer of apparently lytic vesicles from the surface of the strains to the surface of cells, with subsequent digestion of holes in the cell walls. Enzymes associated with these vesicles are likely responsible for the digestion of holes in the cell walls. has potential applications in aquaculture and food safety, in control of the formation of biofilms in the environment, and in food processing. These findings may facilitate the probiotic use of to inactivate pathogens and may lead to the isolation of enzymes and other antimicrobial compounds of pharmacological value.

show abstract

mentioning

confidence: 99%

Mechanisms for Pseudoalteromonas piscicida-Induced Killing of Vibrios and Other Bacterial Pathogens

Richards

Watson

Needleman

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…The presence of maltose as a carbon source in culture media was also shown to enhance protease production by Pseudomonas aeruginosa PseA ( 22 ). In addition, PAP04 protease activity was increased approximately 2.2-fold in the presence of skim milk, reflecting the positive effects of this nitrogen source that have also been shown in Pseudoalteromonas arctica PAMC 21717 ( 23 ) and Bacillus sp. N.40 ( 24 ).…”

Section: Discussionmentioning

confidence: 61%

Enhanced production and organic solvent stability of a protease fromBrevibacillus laterosporus strain PAP04

Anbu

2016

Braz J Med Biol Res

View full text Add to dashboard Cite

A bacterial strain (PAP04) isolated from cattle farm soil was shown to produce an extracellular, solvent-stable protease. Sequence analysis using 16S rRNA showed that this strain was highly homologous (99%) to Brevibacillus laterosporus. Growth conditions that optimize protease production in this strain were determined as maltose (carbon source), skim milk (nitrogen source), pH 7.0, 40°C temperature, and 48 h incubation. Overall, conditions were optimized to yield a 5.91-fold higher production of protease compared to standard conditions. Furthermore, the stability of the enzyme in organic solvents was assessed by incubation for 2 weeks in solutions containing 50% concentration of various organic solvents. The enzyme retained activity in all tested solvents except ethanol; however, the protease activity was stimulated in benzene (74%) followed by acetone (63%) and chloroform (54.8%). In addition, the plate assay and zymography results also confirmed the stability of the PAP04 protease in various organic solvents. The organic solvent stability of this protease at high (50%) concentrations of solvents makes it an alternative catalyst for peptide synthesis in non-aqueous media.

show abstract

“…The protease production of some Pseudoalteromonas strains has been improved by optimization of fermentation conditions or by strain mutagenesis. The production of extracellular protease of P. arctica PAMC 21717 was enhanced 15-fold via statistical optimization of mineral components and fed-batch fermentation (Han et al 2016). Pseudoalteromonas sp.…”

Section: Improvement Of Enzyme Production and Enzyme Stabilitymentioning

confidence: 99%

Proteases from the marine bacteria in the genus Pseudoalteromonas: diversity, characteristics, ecological roles, and application potentials

Chen

Wang

et al. 2020

Mar Life Sci Technol

View full text Add to dashboard Cite

Bacterial strains of the genus Pseudoalteromonas, which includes 48 species, are widely distributed in various ocean environments. Many strains are often abundant and the highest protease producer among marine culturable protease-secreting bacteria, suggesting their important role in marine organic nitrogen degradation and cycling. The extracellular proteases of Pseudoalteromonas are diverse, including serine proteases, metalloproteases, and cystine proteases. Pseudoalteromonas proteases have unique properties, such as cold adaptation, salt tolerance, distinct substrate specificity, and catalytic mechanism. They play important ecological roles in marine organic nitrogen degradation and in the interactions of Pseudoalteromonas with other organisms. Some Pseudoalteromonas proteases have shown promising application potentials in bioactive peptide preparation and meat processing. In this review, advances in our knowledge of Pseudoalteromonas proteases are introduced, with a focus on diversity, characters, ecological significance, and application potentials.

show abstract

Enhanced production of protease by Pseudoalteromonas arctica PAMC 21717 via statistical optimization of mineral components and fed-batch fermentation

Cited by 11 publications

References 37 publications

Mechanisms for Pseudoalteromonas piscicida-Induced Killing of Vibrios and Other Bacterial Pathogens

Mechanisms for Pseudoalteromonas piscicida-Induced Killing of Vibrios and Other Bacterial Pathogens

Enhanced production and organic solvent stability of a protease fromBrevibacillus laterosporus strain PAP04

Proteases from the marine bacteria in the genus Pseudoalteromonas: diversity, characteristics, ecological roles, and application potentials

Contact Info

Product

Resources

About