Molecular screening of Streptomyces isolates for antifungal activity and family 19 chitinase enzymes

Gherbawy, Youssuf A.; Elhariry, Hesham; Altalhi, Abdulla; El-Deeb, Bahig; Khiralla, Ghada M.

doi:10.1007/s12275-012-2095-4

Cited by 39 publications

(27 citation statements)

References 44 publications

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“…3A and B). For both enzymes, degradation products were observed for (GlcNAc) n substrates longer than n ϭ 4 [i.e., (GlcNAc) 4 , (GlcNAc) 5 , and (GlcNAc) 6 ], whereas (GlcNAc) 2 and (GlcNAc) 3 were not hydrolyzed. When using (GlcNAc) 4 as the substrate, the product was (GlcNAc) 2 .…”

Section: Draft Genome Analysis Of T Chitonophagus and Identification Ofmentioning

confidence: 99%

“…(GlcNAc) 5 was converted into (GlcNAc) 3 and (GlcNAc) 2 . When using (GlcNAc) 6 as the substrate, (GlcNAc) 3 and (GlcNAc) 2 were generated.…”

Section: Draft Genome Analysis Of T Chitonophagus and Identification Ofmentioning

confidence: 99%

“…The reaction products were analyzed after centrifugation. Lanes M, standard GlcNAc oligomers ranging from GlcNAc to (GlcNAc) 6 (G1 to G6); lanes b, blank control incubated without enzyme for 36 h at 85°C.…”

Section: Tc-chid(⌬s) or Tc-chid(⌬bd)mentioning

confidence: 99%

“…This would result in T. chitonophagus harboring both kinds of exo-type chitinases along with an endo-type enzyme, and it agrees well with at 85°C for the indicated time periods (0 to 120 min). Lanes M, standard GlcNAc oligomers ranging from GlcNAc to (GlcNAc) 6 (G1 to G6); lanes Mp, standard p-nitrophenyl GlcNAc oligomers ranging from pNP-(GlcNAc) 2 to pNP-(GlcNAc) 5 (pNP-G2 to pNP-G5); lanes b, blank control incubated without enzyme for 120 min at 85°C. the fact that this archaeon displays high levels of chitin degradation among the Archaea.…”

Section: Tc-chid(⌬s) or Tc-chid(⌬bd)mentioning

confidence: 99%

“…These chitinases include enzymes with different substrate specificities that are active toward various states of chitin (4). The GH19 chitinases from Actinomycetes exhibit antifungal activity and have been suggested to play a role in the restriction of fungal growth (4)(5)(6). The chitinolytic machinery of Serratia marcescens, a member of the order Enterobacteriales, has also been extensively studied, leading to the identification of multiple chitinases with different catalytic properties (7).…”

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confidence: 99%

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A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus

Horiuchi

Aslam

Kanai

et al. 2016

Appl Environ Microbiol

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A structurally novel chitinase, Tc-ChiD, was identified from the hyperthermophilic archaeon Thermococcus chitonophagus, which can grow on chitin as the sole organic carbon source. The gene encoding Tc-ChiD contains regions corresponding to a signal sequence, two chitin-binding domains, and a putative catalytic domain. This catalytic domain shows no similarity with previously characterized chitinases but resembles an uncharacterized protein found in the mesophilic anaerobic bacterium Clostridium botulinum. Two recombinant Tc-ChiD proteins were produced in Escherichia coli, one without the signal sequence [TcChiD(⌬S)] and the other corresponding only to the putative catalytic domain [Tc-ChiD(⌬BD)]. Enzyme assays using N-acetylglucosamine (GlcNAc) oligomers indicated that both proteins hydrolyze GlcNAc oligomers longer than (GlcNAc) 4 . Chitinase assays using colloidal chitin suggested that Tc-ChiD is an exo-type chitinase that releases (GlcNAc) 2 or (GlcNAc) 3 . Analysis with GlcNAc oligomers modified with p-nitrophenol suggested that Tc-ChiD recognizes the reducing end of chitin chains. While TcChiD(⌬BD) displayed a higher initial velocity than that of Tc-ChiD(⌬S), we found that the presence of the two chitin-binding domains significantly enhanced the thermostability of the catalytic domain. In T. chitonophagus, another chitinase ortholog that is similar to the Thermococcus kodakarensis chitinase ChiA is present and can degrade chitin from the nonreducing ends. Therefore, the presence of multiple chitinases in T. chitonophagus with different modes of cleavage may contribute to its unique ability to efficiently degrade chitin. IMPORTANCEA structurally novel chitinase, Tc-ChiD, was identified from Thermococcus chitonophagus, a hyperthermophilic archaeon. The protein contains a signal peptide for secretion, two chitin-binding domains, and a catalytic domain that shows no similarity with previously characterized chitinases. Tc-ChiD thus represents a new family of chitinases. Tc-ChiD is an exo-type chitinase that recognizes the reducing end of chitin chains and releases (GlcNAc) 2 or (GlcNAc) 3 . As a thermostable chitinase that recognizes the reducing end of chitin chains was not previously known, Tc-ChiD may be useful in a wide range of enzyme-based technologies to degrade and utilize chitin. Chitin is a ␤-1,4-linked insoluble linear polymer of N-acetylglucosamine (GlcNAc) and is the main component of the exoskeleton of crustaceans and insects, as well as the cell walls of fungi. Chitin is the second most abundant natural polysaccharide after cellulose, and its annual formation rate is in the order of 10 10 to 10 11 tons (1). At present, the majority of chitin remains unused, and thus the development of effective methods to convert chitin into useful biomaterials and/or bioenergy is important to maintain our supplies of edible polysaccharides, such as starch.Chitinases are enzymes responsible for the hydrolysis of chitin polymer, and they produce GlcNAc and/or its oligomers as products. Chitinases are found ...

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Section: Draft Genome Analysis Of T Chitonophagus and Identification Ofmentioning

confidence: 99%

“…(GlcNAc) 5 was converted into (GlcNAc) 3 and (GlcNAc) 2 . When using (GlcNAc) 6 as the substrate, (GlcNAc) 3 and (GlcNAc) 2 were generated.…”

Section: Draft Genome Analysis Of T Chitonophagus and Identification Ofmentioning

confidence: 99%

Section: Tc-chid(⌬s) or Tc-chid(⌬bd)mentioning

confidence: 99%

Section: Tc-chid(⌬s) or Tc-chid(⌬bd)mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus

Horiuchi

Aslam

Kanai

et al. 2016

Appl Environ Microbiol

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Microbial Chitinases and Their Applications: An Overview

Nayak

Mohanty

et al. 2021

Environmental and Agricultural Microbiology

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Isolation and evaluation of endophytic Streptomyces endusOsiSh‐2 with potential application for biocontrol of rice blast disease

Zeng

et al. 2016

J Sci Food Agric

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Molecular screening of Streptomyces isolates for antifungal activity and family 19 chitinase enzymes

Cited by 39 publications

References 44 publications

A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus

A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus

Microbial Chitinases and Their Applications: An Overview

Isolation and evaluation of endophytic Streptomyces endusOsiSh‐2 with potential application for biocontrol of rice blast disease

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