Characterization and optimization of heterologous expression in Escherichia coli of the chitinase encoded by the chiA gene of Bacillus halodurans C-125

Silva, Abigail F. da; García-Fraga, Belén; López-Seijas, Jacobo; Sieiro, Carmen

doi:10.1016/j.procbio.2014.06.020

Cited by 15 publications

(11 citation statements)

References 38 publications

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“…The 38 amino acids located at the N-terminus were predicted to be a signal peptide for protein export. The sequence F 152 EGIDIDYE 160 shows high similarity to the pattern from the PROSITE database for the active-site consensus sequence: [LIVMFY]-[DN]-G-[LIVMF]-[DN]-[LIVMF]-[DN]-x-E, where E is the active-site residue [ 21 ]. A fibronectin type III domain (FnIIID), described in many chitinase studies, was identified in amino acids P 103 and T 186 .…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland

Liu

Cheng

Miao

2015

Genes

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To isolate and characterize chitinases that can be applied with practical advantages, 57 isolates of chitin-degrading bacteria were isolated from the soil of a suburban wetland. 16S rRNA gene analysis revealed that the majority of these strains belonged to two genera, Paenibacillus and Brevibacillus. Taking thermostability into account, the chitinases (ChiA and ChiC) of a B. laterosporus strain were studied further. Ni-NTA affinity-purified ChiA and ChiC were optimally active at pH 7.0 and 6.0, respectively, and showed high temperature stability up to 55 °C. Kinetic analysis revealed that ChiC has a lower affinity and stronger catalytic activity toward colloidal chitin than ChiA. With their stability in a broad temperature range, ChiA and ChiC can be utilized for the industrial bioconversion of chitin wastes into biologically active products.

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Section: Resultsmentioning

confidence: 99%

“…In this study, the optimum temperature of ChiA and ChiC ranged from 55 °C to 60 °C; ChiA remained stable up to 60 °C. These two enzymes are more stable than the recently described chitinases from Bacillus halodurans [ 21 ], Stenotrophomonas maltophilia [ 39 ], and Streptomyces sp. [ 36 ].…”

Section: Discussionmentioning

confidence: 99%

Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland

Liu

Cheng

Miao

2015

Genes

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“…Both Fn3 proteins were also upregulated in response to GMP, as were several other hypothetical genes in the clusters. The Fn3 domains have previously been described in several bacterial glycoside hydrolases (Little et al, 1994;da Silva et al, 2014). These domains may have a role in the degradation of insoluble substrates and may have been acquired by bacteria through horizontal gene transfer from animals (da Silva et al, 2014).…”

Section: Effect Of Gmp Treatment On Carbohydrate-related Genesmentioning

confidence: 99%

Bovine glycomacropeptide promotes the growth of Bifidobacterium longum ssp. infantis and modulates its gene expression

O’Riordan

O’Callaghan

Buttó

et al. 2018

Journal of Dairy Science

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Bovine milk glycomacropeptide (GMP) is derived from κ-casein, with exclusively o-linked glycosylation. Glycomacropeptide promoted the growth of Bifidobacterium longum ssp. infantis in a concentration-dependent manner, and this activity was lost following periodate treatment of the GMP (GMP-P), which disables biological recognition of the conjugated oligosaccharides. Transcriptional analysis of B. longum ssp. infantis following exposure to GMP revealed a substantial response to GMP relative to bacteria treated with GMP-P, with a greater number of differentially expressed transcripts and larger fold changes versus the control. Therefore, stimulation of B. longum ssp. infantis growth by GMP is intrinsically linked to the peptide's O-linked glycosylation. The pool of differentially expressed transcripts included 2 glycoside hydrolase (family 25) genes, which were substantially upregulated following exposure to GMP, but not GMP-P. These GH25 genes were present in duplicated genomic islands that also contained genes encoding fibronectin type III binding domain proteins and numerous phage-related proteins, all of which were also upregulated. Homologs of this genomic arrangement were present in other Bifidobacterium species, which suggest it may be a conserved domain for the utilization of glycosylated peptides. This study provides insights into the molecular basis for the prebiotic effect of bovine milk GMP on B. longum ssp. infantis.

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“…Murein is the basic component of the bacterial cell wall and consists of cross-linked peptide chains with repeating GlcNAc and muramic acid residues [35,36]. HA is a linear heteropolysaccharide that is composed of repeating D-glucuronic acid and GlcNAc residues.…”

Section: Glycan Biosynthesismentioning

confidence: 99%

Bacterial chitinase: nature and perspectives for sustainable bioproduction

Yan

Fong

2015

Bioresour. Bioprocess.

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Concurrent advances in a number of fields have fostered the development of bioprocesses for biochemical production. Ideally, future bioprocesses will meet the demands of commercial chemical markets in an economical fashion while being sustainable through the use of renewable starting materials. A number of different renewable and abundant biopolymers (e.g., cellulose, hemicelluloses, lignin, and chitin) are potential starting material for sustainable bioprocesses, but a broad challenge remains on how to efficiently depolymerize these biopolymers to generate monomeric sugars that can be metabolized by industrial microorganisms or other useful building block chemicals. Indeed, a variety of specialty chemicals may be able to be generated from these various monomers. This review focuses on the biopolymer chitin and discusses research and knowledge relevant to chitin degradation and potential chemical products that can be made from chitin degradation products.

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Characterization and optimization of heterologous expression in Escherichia coli of the chitinase encoded by the chiA gene of Bacillus halodurans C-125

Cited by 15 publications

References 38 publications

Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland

Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland

Bovine glycomacropeptide promotes the growth of Bifidobacterium longum ssp. infantis and modulates its gene expression

Bacterial chitinase: nature and perspectives for sustainable bioproduction

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