ArticleExtremophiles : life under extreme conditions2008
Molecular analysis of the gene encoding a new chitinase from the marine psychrophilic bacterium Moritella marina and biochemical characterization of the recombinant enzyme.
Article in Extremophiles : life under extreme conditions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 55 citations in OpenAlex.
- Niche separation in bacterial communities and activities in porewater, loosely attached, and firmly attached fractions in permeable surface sediments.The ISME journal · 2024Article
- Microbial chitinases and their relevance in various industries.Folia microbiologica · 2023Review
- Marine Bioprospecting, Biocatalysis and Process Development.Microorganisms · 2022Review
- Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin intoMarine drugs · 2022Article
- Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles' Heel in Protein Structure and Industrial Utilization.Molecules (Basel, Switzerland) · 2021Article
- Comparative Genomic Study of Polar Lichen-Associated Hymenobacter sp. PAMC 26554 and Hymenobacter sp. PAMC 26628 Reveals the Presence of Polysaccharide-Degrading Ability Based on Habitat.Current microbiology · 2020Article
- Extremophile - An Adaptive Strategy for Extreme Conditions and Applications.Current genomics · 2020Review
- Structural Insight Into Chitin Degradation and Thermostability of a Novel Endochitinase From the Glycoside Hydrolase Family 18.Frontiers in microbiology · 2019Article
- Review
- Characterization of a cold-adapted and salt-tolerant exo-chitinase (ChiC) from Pseudoalteromonas sp. DL-6.Extremophiles : life under extreme conditions · 2016Article
- Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Scientific reports · 2015Article
- The stability of the TIM-barrel domain of a psychrophilic chitinase.Biochemistry and biophysics reports · 2015Article
- Characterization of an extracellular thermophilic chitinase from Paenibacillus thermoaerophilus strain TC22-2b isolated from compost.World journal of microbiology & biotechnology · 2015Article
- Draft genome sequence of Arctic marine Bacterium Pseudoalteromonas issachenkonii PAMC 22718.Journal of bacteriology · 2012Article
- Structural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function.Journal of computer-aided molecular design · 2012Article
- Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12.Microbial cell factories · 2011Article
- The importance of chitin in the marine environment.Marine biotechnology (New York, N.Y.) · 2011Article
- Biotechnological uses of enzymes from psychrophiles.Microbial biotechnology · 2011Review
- A Chitinase from Aeromonas veronii CD3 with the potential to control myxozoan disease.PloS one · 2011Article
- Molecular cloning and stress-dependent expression of a gene encoding Delta(12)-fatty acid desaturase in the Antarctic microalga Chlorella vulgaris NJ-7.Extremophiles : life under extreme conditions · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The marine psychrophilic bacterium Moritella marina, isolated from a sample raised from a depth of 1,200 m in the northern Pacific Ocean, secretes several chitinases in response to chitin induction. A gene coding for an extracellular chitinolytic enzyme was cloned and its nucleotide sequence was determined. The chitinase gene consists of an open reading frame of 1,650 nucleotides and encodes a protein of 550 amino acids with a calculated molecular weight of 60.788 kDa, named MmChi60. MmChi60 has a modular structure consisting of a glycosyl-hydrolase family 18 N-terminal catalytic region as well as a C-terminal chitin-binding domain (ChBD). The new chitinase was purified to homogeneity from the intracellular fraction of Escherichia coli. The optimum pH and temperature of the recombinant MmChi60 were 5.0 and 28 degrees C, respectively. The mode of action of the new enzyme on N-acetylchitooligomers, chitin polymers, and other substrates was examined, and MmChi60 was classified as an endochitinase. Thermal unfolding of MmChi60 was studied using differential scanning microcalorimetry and revealed that the protein unfolds reversibly at 65 degrees C. On the basis of the crystal structure of the chitinase C of Streptomyces griseus, a homology-based 3-D model of the ChBD of the MmChi60 was calculated.
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