Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca

Gaber, Yasser; Mekasha, Sophanit; Vaaje‐Kolstad, Gustav; Eijsink, Vincent G. H.; Fraaije, Marco W.

doi:10.1016/j.bbapap.2016.04.010

Cited by 22 publications

(11 citation statements)

References 41 publications

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“…The purified Tfu_0580 activity (2.75 ± 0.32 mU/mg protein) against colloidal chitin is comparable to that of the Streptomyces griseus chitinase (4.41 ± 0.72 mU/mg protein). In contrast to the finding of no obvious chitinase activity of Tfu_0868 against colloidal chitin reported in a recent study [ 26 ], our results showed the first evidence of chitinase activity against colloidal chitin in T. fusca . Compared to the reported predicted functional active sites (Gln289 and Ser263) of Tfu_0868 [ 26 ], the equivalent active sites of Tfu_0580 are Gln and Tyr.…”

Section: Resultscontrasting

confidence: 99%

“…In contrast to the finding of no obvious chitinase activity of Tfu_0868 against colloidal chitin reported in a recent study [ 26 ], our results showed the first evidence of chitinase activity against colloidal chitin in T. fusca . Compared to the reported predicted functional active sites (Gln289 and Ser263) of Tfu_0868 [ 26 ], the equivalent active sites of Tfu_0580 are Gln and Tyr. It was found that Gln289 and Ser263 of Tfu_0868 lead to weak chitinase activity, however, the Arthrobacter sp.…”

Section: Resultscontrasting

confidence: 99%

“…After search in the T. fusca genomic information, two open reading frames ( tfu_0580 , GI: AAZ54618 and tfu_0868 , GI: AAZ54906) are found with an annotation of chitinases. Recently, Tfu_0868 has been cloned and overexpressed in Escherichia coli [ 26 ]. The enzyme was found to be relatively thermostable at 57.5 °C and the optimum temperature being 40–45 °C.…”

Section: Introductionmentioning

confidence: 99%

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Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase

Yan

Fong

2018

Biotechnology Reports

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Section: Resultscontrasting

confidence: 99%

Section: Resultscontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase

Yan

Fong

2018

Biotechnology Reports

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“…Actinomycetes viz. Thermobifida fusca [42], Streptomyces pratensis [43], and Saccharothrix yanglingensis [44] have also been reported to produce notable levels of chitinase. Bacteria primarily produce chitinases in order to degrade chitin for its utilization as an energy source, whereas some bacterial chitinases have shown potentiality as biological control agents against a variety of plant diseases caused by phytopathogenic fungi [45][46][47].…”

Section: Chitinases From Microorganismsmentioning

confidence: 99%

Chitinases—Potential Candidates for Enhanced Plant Resistance towards Fungal Pathogens

et al. 2018

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Crop cultivation is crucial for the existence of human beings, as it fulfills our nutritional requirements. Crops and other plants are always at a high risk of being attacked by phytopathogens, especially pathogenic fungi. Although plants have a well-developed defense system, it can be compromised during pathogen attack. Chitinases can enhance the plant's defense system as they act on chitin, a major component of the cell wall of pathogenic fungi, and render the fungi inactive without any negative impact on the plants. Along with strengthening plant defense mechanisms, chitinases also improve plant growth and yield. Chitinases in combination with recombinant technology can be a promising tool for improving plant resistance to fungal diseases. The applicability of chitinase-derived oligomeric products of chitin further augment chitinase prospecting to enhance plant defense and growth.

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“…Nevertheless, there are organisms possessing genes coding for chitinolytic enzymes but not growing on chitin-containing culture media. Notable examples include the erythromycin producer Saccharopolyspora erythraea and the potent cellulose degrader Thermobifida fusca (Gaber et al 2016; Liao et al 2014). …”

Section: Chitinolytic Properties Of Actinobacteriamentioning

confidence: 99%

Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution

Lacombe-Harvey

Brzeziński

Beaulieu

2018

Appl Microbiol Biotechnol

110

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Actinobacteria, a large group of Gram-positive bacteria, secrete a wide range of extracellular enzymes involved in the degradation of organic compounds and biopolymers including the ubiquitous aminopolysaccharides chitin and chitosan. While chitinolytic enzymes are distributed in all kingdoms of life, actinobacteria are recognized as particularly good decomposers of chitinous material and several members of this taxon carry impressive sets of genes dedicated to chitin and chitosan degradation. Degradation of these polymers in actinobacteria is dependent on endo- and exo-acting hydrolases as well as lytic polysaccharide monooxygenases. Actinobacterial chitinases and chitosanases belong to nine major families of glycosyl hydrolases that share no sequence similarity. In this paper, the distribution of chitinolytic actinobacteria within different ecosystems is examined and their chitinolytic machinery is described and compared to those of other chitinolytic organisms.Electronic supplementary materialThe online version of this article (10.1007/s00253-018-9149-4) contains supplementary material, which is available to authorized users.

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Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca

Cited by 22 publications

References 41 publications

Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase

Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase

Chitinases—Potential Candidates for Enhanced Plant Resistance towards Fungal Pathogens

Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution

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