Transgenic tobacco plants expressing endo-β-mannanase gene from deep-sea Bacillus sp. JAMB-602 strain confer enhanced resistance against fungal pathogen (Fusarium oxysporum)

Hoshikawa, Ken; Endo, Satoshi; Mizuniwa, Shingo; Makabe, So; Takahashi, Hiroyuki; Nakamura, Ikuo

doi:10.1007/s11816-012-0219-2

Cited by 7 publications

(5 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore β-1, 3-glucanases are involved in the degradation of fungal cell walls and may provide chitinolytic bacteria with an additional defense mechanism against fungi (Aono et al, 1992;Arora et al, 2007;Hoshikawa et al, 2012). Therefore β-1, 3-glucanases are involved in the degradation of fungal cell walls and may provide chitinolytic bacteria with an additional defense mechanism against fungi (Aono et al, 1992;Arora et al, 2007;Hoshikawa et al, 2012).…”

Section: Occurrence Of Other Proteins Possibly Related To Anti-fungalmentioning

confidence: 99%

“…Next to chitin, fungal cell walls contain different polysaccharides, such as β-1,3-glucan. Therefore β-1, 3-glucanases are involved in the degradation of fungal cell walls and may provide chitinolytic bacteria with an additional defense mechanism against fungi (Aono et al, 1992;Arora et al, 2007;Hoshikawa et al, 2012). Yet, the frequency of β-1,3-glucanases was low in both aquatic and terrestrial chitinase-containing bacterial genomes with the exception of genomes of terrestrial Actinobacteria (Table 3).…”

Section: Occurrence Of Other Proteins Possibly Related To Anti-fungalmentioning

confidence: 99%

See 1 more Smart Citation

Genomic comparison of chitinolytic enzyme systems from terrestrial and aquatic bacteria

Bai

Eijsink

Kielak

et al. 2014

Environmental Microbiology

View full text Add to dashboard Cite

Chitin degradation ability is known for many aquatic and terrestrial bacterial species. However, differences in the composition of chitin resources between aquatic (mainly exoskeletons of crustaceans) and terrestrial (mainly fungal cell walls) habitats may have resulted in adaptation of chitinolytic enzyme systems to the prevalent resources. We screened publicly available terrestrial and aquatic chitinase-containing bacterial genomes for possible differences in the composition of their chitinolytic enzyme systems. The results show significant differences between terrestrial and aquatic bacterial genomes in the modular composition of chitinases (i.e. presence of different types of carbohydrate binding modules). Terrestrial Actinobacteria appear to be best adapted to use a wide variety of chitin resources as they have the highest number of chitinase genes, the highest diversity of associated carbohydrate-binding modules and the highest number of CBM33-type lytic polysaccharide monooxygenases. Actinobacteria do also have the highest fraction of genomes containing β-1, 3-glucanases, enzymes that may reinforce the potential for degrading fungal cell walls. The fraction of bacterial chitinase-containing genomes encoding polyketide synthases was much higher for terrestrial bacteria than for aquatic ones supporting the idea that the combined production of antibiotics and cell-wall degrading chitinases can be an important strategy in antagonistic interactions with fungi.

show abstract

Section: Occurrence Of Other Proteins Possibly Related To Anti-fungalmentioning

confidence: 99%

Section: Occurrence Of Other Proteins Possibly Related To Anti-fungalmentioning

confidence: 99%

Genomic comparison of chitinolytic enzyme systems from terrestrial and aquatic bacteria

Bai

Eijsink

Kielak

et al. 2014

Environmental Microbiology

View full text Add to dashboard Cite

show abstract

“…Almost all genetically modified (GM) plant products are derived from seeds. Although endoglucanases (Gray et al ., ; Harrison et al ., ), exoglucanase (Harrison et al ., , ), mannanase (Agrawal et al ., ; Hoshikawa et al ., ) and lipase (Gruber et al ., ; Lakshmi et al ., ; Pereira et al ., ) have been expressed in leaves, no leaf‐based protein/enzyme commercial product has been launched so far. Therefore, in this study, we report production of lipase, mannanase, endoglucanase and exoglucanase in tobacco or lettuce chloroplasts, characterization of enzyme activity at different pH and temperature in crude leaf extracts without need for purification, stability over long‐term storage of dried plant cells at ambient temperature and efficacy validation of stain removal, biowashing and biopolishing, when compared with current microbial products in detergent or textile industries.…”

Section: Introductionmentioning

confidence: 99%

Validation of leaf enzymes in the detergent and textile industries: launching of a new platform technology

Kumari

Singh

Ray

et al. 2019

Plant Biotechnology Journal

View full text Add to dashboard Cite

Summary Chemical catalysts are being replaced by biocatalysts in almost all industrial applications due to environmental concerns, thereby increasing their demand. Enzymes used in current industries are produced in microbial systems or plant seeds. We report here five newly launched leaf‐enzyme products and their validation with 15 commercial microbial‐enzyme products, for detergent or textile industries. Enzymes expressed in chloroplasts are functional at broad pH /temperature ranges as crude‐leaf extracts, while most purified commercial enzymes showed significant loss at alkaline pH or higher temperature, required for broad range commercial applications. In contrast to commercial liquid enzymes requiring cold storage/transportation, chloroplast enzymes as a leaf powder can be stored up to 16 months at ambient temperature without loss of enzyme activity. Chloroplast‐derived enzymes are stable in crude‐leaf extracts without addition of protease inhibitors. Leaf lipase/mannanase crude extracts removed chocolate or mustard oil stains effectively at both low and high temperatures. Moreover, leaf lipase or mannanase crude‐extracts removed stain more efficiently at 70 °C than commercial microbial enzymes (<10% activity). Endoglucanase and exoglucanase in crude leaf extracts removed dye efficiently from denim surface and depilled knitted fabric by removal of horizontal fibre strands. Due to an increased demand for enzymes in the food industry, marker‐free lettuce plants expressing lipase or cellobiohydrolase were created for the first time and site‐specific transgene integration/homoplasmy was confirmed by Southern blots. Thus, leaf‐production platform offers a novel low‐cost approach by the elimination of fermentation, purification, concentration, formulation and cold‐chain storage/transportation. This is the first report of commercially launched protein products made in leaves and validated with current commercial products.

show abstract

“…Seeds were surface sterilized and cultured on half-strength MS medium. Leaf explants of ten-days-old seedlings of tomato and tobacco (Nicotiana tabacum 'Petite Havana' SR1) were used for Agrobacterium-mediated transformation as previously described by Hoshikawa et al (2012a).…”

Section: Regeneration Of Transgenic Plantmentioning

confidence: 99%

Transgenic tobacco and tomato plants expressing Wasabi defensin genes driven by root-specific LjNRT2 and AtNRT2.1 promoters confer resistance against Fusarium oxysporum

Kong

Ntui

Makabe

et al. 2014

Plant Biotechnology

Self Cite

View full text Add to dashboard Cite

Antifungal peptides are a potential group of defense molecules that have been utilized to develop resistance to various plant pathogens. Wasabi defensin (WD) gene (0.5 kb) consists of cysteine-rich peptides that show potent growth inhibition of pathogenic filamentous fungi, such as Botrytis cinerea. Under regulation by the root-specific LjNRT2 or AtNRT2.1 promoter, WD gene was expressed in the roots of transgenic tobacco and tomato plants by Agrobacteriummediated transformation. The regenerated plants showed stable integration of the transgene, with different insertion sites, and the transgene was expressed in the root tissues but not in the leaf tissues. This result confirmed that WD protein accumulated only in the roots of transgenic plants. In a bioassay for resistance to Fusarium oxysporum, all transgenic plants showed increased resistance to the fungus as compared to non-transformed plants. Protein extracts from root and leaf tissues were assayed for antifungal activity and the activity was express as the number of colonies formed per cm 2 (CFU cm −2 ). The CFU values of the root and leaf extracts of control plants did not show significant differences. In contrast, the CFU values of the root extracts of the transgenic plants were significantly lower than those of the leaf extracts and much lower than those of control. These results suggest that LjNRT2 and AtNRT2.1 promoters triggered the antifungal gene expression in the roots and conferred increased resistance to the root pathogen F. oxysporum. In the view of bio-safety, the root-specific expression of the transgene is desirable because the roots of tomato are not edible.

show abstract

Transgenic tobacco plants expressing endo-β-mannanase gene from deep-sea Bacillus sp. JAMB-602 strain confer enhanced resistance against fungal pathogen (Fusarium oxysporum)

Cited by 7 publications

References 31 publications

Genomic comparison of chitinolytic enzyme systems from terrestrial and aquatic bacteria

Genomic comparison of chitinolytic enzyme systems from terrestrial and aquatic bacteria

Validation of leaf enzymes in the detergent and textile industries: launching of a new platform technology

Transgenic tobacco and tomato plants expressing Wasabi defensin genes driven by root-specific LjNRT2 and AtNRT2.1 promoters confer resistance against Fusarium oxysporum

Contact Info

Product

Resources

About