ArticleMicrobial cell factories2011
Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12.
Article in Microbial cell factories, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 79 citations in OpenAlex.
- Review
- Article
- Cloning, expression, purification, and mutant construction of the chitinase PbCHI2 gene from Photobacterium sp.Archives of microbiology · 2025Article
- A novel antifungal chitinase from Chaetomium globosum: column-free purification and characterization.Archives of microbiology · 2025Article
- Genomics, Proteomics, and Antifungal Activity of Chitinase from the Antarctic Marine BacteriumInternational journal of molecular sciences · 2024Article
- An overview of fungal chitinases and their potential applications.Protoplasma · 2023Review
- Microbial chitinases and their relevance in various industries.Folia microbiologica · 2023Review
- Identification of Exoenzymes Secreted by Entomopathogenic FungusJournal of fungi (Basel, Switzerland) · 2022Article
- Cold-Active Enzymes and Their Potential Industrial Applications-A Review.Molecules (Basel, Switzerland) · 2022Review
- Isolation of Chitinolytic Bacteria from European Sea Bass Gut Microbiota Fed Diets with Distinct Insect Meals.Biology · 2022Article
- Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin intoMarine drugs · 2022Article
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Two Highly Similar Chitinases from MarineMarine drugs · 2020Article
- Article
- High-level expression, purification and properties of an Endochitinase gene without signal peptide from Lecanicillium lecanii 43H in Pichia pastoris.Molecular biology reports · 2018Article
- Biochemical and structural characterization of a novel cold-active esterase-like protein from the psychrophilic yeast Glaciozyma antarctica.Extremophiles : life under extreme conditions · 2018Article
- Complete genome ofStandards in genomic sciences · 2017Article
- Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Characterization of a cold-adapted and salt-tolerant exo-chitinase (ChiC) from Pseudoalteromonas sp. DL-6.Extremophiles : life under extreme conditions · 2016Article
- Current Technological Improvements in Enzymes toward Their Biotechnological Applications.Frontiers in microbiology · 2016Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCold-adapted enzymes are proteins produced by psychrophilic organisms that display a high catalytic efficiency at extremely low temperatures. Chitin consists of the insoluble homopolysaccharide β-(1, 4)-linked N-acetylglucosamine, which is the second most abundant biopolymer found in nature. Chitinases (EC 3.2.1.14) play an important role in chitin recycling in nature. Biodegradation of chitin by the action of cold-adapted chitinases offers significant advantages in industrial applications such as the treatment of chitin-rich waste at low temperatures, the biocontrol of phytopathogens in cold environments and the biocontrol of microbial spoilage of refrigerated food.
resultsA gene encoding a cold-adapted chitinase (CHI II) from Glaciozyma antarctica PI12 was isolated using Rapid Amplification of cDNA Ends (RACE) and RT-PCR techniques. The isolated gene was successfully expressed in the Pichia pastoris expression system. Analysis of the nucleotide sequence revealed the presence of an open reading frame of 1,215 bp, which encodes a 404 amino acid protein. The recombinant chitinase was secreted into the medium when induced with 1% methanol in BMMY medium at 25°C. The purified recombinant chitinase exhibited two bands, corresponding to the non-glycosylated and glycosylated proteins, by SDS-PAGE with molecular masses of approximately 39 and 50 kDa, respectively. The enzyme displayed an acidic pH characteristic with an optimum pH at 4.0 and an optimum temperature at 15°C. The enzyme was stable between pH 3.0-4.5 and was able to retain its activity from 5 to 25°C. The presence of K+, Mn2+ and Co2+ ions increased the enzyme activity up to 20%. Analysis of the insoluble substrates showed that the purified recombinant chitinase had a strong affinity towards colloidal chitin and little effect on glycol chitosan. CHI II recombinant chitinase exhibited higher Vmax and Kcat values toward colloidal chitin than other substrates at low temperatures.
conclusionBy taking advantage of its high activity at low temperatures and its acidic pH optimum, this recombinant chitinase will be valuable in various biotechnological applications under low temperature and acidic pH conditions.
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