Production, characterization, gene cloning, and nematocidal activity of the extracellular protease from  Stenotrophomonas maltophilia  N4

Jankiewicz, Urszula; Larkowska, Ewa; Brzezinska, Maria Swiontek

doi:10.1016/j.jbiosc.2015.11.011

Cited by 25 publications

(18 citation statements)

References 29 publications

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“…KerSMF keratinase was found to exhibit a biocidal activity on the nematodes, Caenorhabditis elegans and Panagrellus spp. [ 66 ], which makes it an efficient biocontrol agent for plant-parasitic nematodes [ 67 ]. As was shown by Dunne et al [ 68 ], the mutant of S. maltophilia W81 that was unable to produce one of the extracellular proteases failed to efficiently control the pathogenic fungus Pythium ultimum .…”

Section: Discussionmentioning

confidence: 99%

Comparative Genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila Revealed Characteristic Features of Both Species

Piński

Żur

Hasterok

et al. 2020

IJMS

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Although Stenotrophomonas maltophilia strains are efficient biocontrol agents, their field applications have raised concerns due to their possible threat to human health. The non-pathogenic Stenotrophomonas rhizophila species, which is closely related to S. maltophilia, has been proposed as an alternative. However, knowledge regarding the genetics of S. rhizophila is limited. Thus, the aim of the study was to define any genetic differences between the species and to characterise their ability to promote the growth of plant hosts as well as to enhance phytoremediation efficiency. We compared 37 strains that belong to both species using the tools of comparative genomics and identified 96 genetic features that are unique to S. maltophilia (e.g., chitin-binding protein, mechanosensitive channels of small conductance and KGG repeat-containing stress-induced protein) and 59 that are unique to S. rhizophila (e.g., glucosylglycerol-phosphate synthase, cold shock protein with the DUF1294 domain, and pteridine-dependent dioxygenase-like protein). The strains from both species have a high potential for biocontrol, which is mainly related to the production of keratinases (KerSMD and KerSMF), proteinases and chitinases. Plant growth promotion traits are attributed to the biosynthesis of siderophores, spermidine, osmoprotectants such as trehalose and glucosylglycerol, which is unique to S. rhizophila. In eight out of 37 analysed strains, the genes that are required to degrade protocatechuate were present. While our results show genetic differences between the two species, they had a similar growth promotion potential. Considering the information above, S. rhizophila constitutes a promising alternative for S. maltophilia for use in agricultural biotechnology.

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Section: Discussionmentioning

confidence: 99%

Comparative Genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila Revealed Characteristic Features of Both Species

Piński

Żur

Hasterok

et al. 2020

IJMS

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“…Generally, all of the proteins can be precipitated using acetone 20-50% (Scopes, 1987). Chitinase of Stenotrophomonas maltophilia and Penicillium ochrochloronwere successfully precipitated using 70% acetone (Patil et al, 2013;Jankiewicz and Brzezinska, 2015).…”

Section: Discussionmentioning

confidence: 99%

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

Azizah¹,

Mubarik²,

Sudirman³

2015

Research J. of Microbiology

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The objective of this research was to screen and identify of chitinolytic bacteria which have an ability to inhibit the growth of G. boninense and also to characterize its chitinase activity on degrading the chitin of G. boninense. Screening of chitinolytic bacteria against G. boninense by using dual culture method on Potato Dextrose Agar (PDA) showed that bacterial isolates SAHA 12.07 and KAHN 15.12 had the highest percentage inhibition of 68,19 and 40, 29%, respectively. Based on 16S rRNA identifications, SAHA 12.07 and KAHN 15.12 were identified as Bacillus amyloliquefaciens and Serratia marcescens, respectively. Isolate SAHA 12.07 produced optimum chitinase at 48 h and KAHN 15.12 at 54 h of incubation in chitin medium. Crude chitinase of SAHA 12.07 and KAHN 15.12 have precipitated by acetone at 60 and 20%, respectively. Chitinase activity had active at pH 4-10 and temperature about 20-80°C. In vitro lysis of G. boninense bioassay showed that the chitinase of SAHA 12.07 and KAHN 15.12 were capable to inhibit the growth of mycelium G. boninense and could release of N-acetylglucosamine by incubation of G. boninense with partially purified enzyme.

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“…The presence of SDS and Triton X-100 inhibited the activity of the enzyme by 25 and 5%, respectively. The studied bacterium S. maltophilia N4 is very interesting in view of its wealth of extracellular hydrolases as well as characterized chitinolytic activity (Jankiewicz & Swiontek Brzezinska, 2015;Jankiewicz et al, 2016) and the current study deals with proteases showing keratinolytic activity. The obtained results point to a close dependence between the activity of the bacterial proteases and the composition of the culture medium.…”

Section: And Ms Analysismentioning

confidence: 99%

Identification and properties of a keratinase from Stenotrophomonas maltophilia N4 with potential application in biotechnology

Jankiewicz

Frąk

2018

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Proteolytic enzymes, also known as peptidases, proteases or proteinases, have always been a relevant and valid study subject. The considerable interest in bacterial proteolytic enzymes largely results from the possibilities of their application. Such enzymes are commonly used in biotechnology due to their biochemical diversity, high stability under unfavorable reaction conditions, relatively low cost of obtaining, and the ease of their genetic manipulation 2015). The enzymes, which hydrolyze peptide bonds that link amino acids together in the polypeptide chain forming a protein, may be used to remove protein waste, particularly including protein waste that is insoluble in water and therefore degrades more slowly in the natural environment.

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Production, characterization, gene cloning, and nematocidal activity of the extracellular protease from Stenotrophomonas maltophilia N4

Cited by 25 publications

References 29 publications

Comparative Genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila Revealed Characteristic Features of Both Species

Comparative Genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila Revealed Characteristic Features of Both Species

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

Identification and properties of a keratinase from Stenotrophomonas maltophilia N4 with potential application in biotechnology

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