Microbial chitinases: properties, current state and biotechnological applications

Le, Bao; Yang, Seung-Hwan

doi:10.1007/s11274-019-2721-y

Cited by 77 publications

(46 citation statements)

References 102 publications

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“…Various investigations reported that chitinolytic enzyme produced from S. marcescens and Pichia kudriavzevii, degraded chitin and produced SCPs. The yield of generated single cell proteins was 45% protein and 8-11% nucleic acids [86].…”

Section: Production Of Single Cell Proteinmentioning

confidence: 98%

“…Single cell proteins (SCP) can be utilized as a protein dietary additive and can reinstate expensive traditional protein sources such as fish meal and soymeal [85,86]. Shell fish waste is an abundant source of calcium carbonate, protein and chitin.…”

Section: Production Of Single Cell Proteinmentioning

confidence: 99%

“…Chitinase from Penicillium ochrochloron MTCC 517 and Yarrnowia lipolytica NCIM 3450 was used for hydrolysis of chitin and generation of N-Acetyl-D-glucosamine and SCPs. It was found that chitin (2%) provided optimum yield of SCP with a maximum yield of 2.9% nucleic acid and 65% protein, from biomass of 9.4 g/l [86,87].…”

Section: Production Of Single Cell Proteinmentioning

confidence: 99%

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Distribution and Biotechnological Applications of Chitinase: A Review

Dukariya¹,

Kumar²

2020

ijbb

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Chitinases are a group of hydrolytic enzymes catalysing degradation of chitin, the second most abundant polysaccharide in nature. Chitin is an essential structural component of most fungi cell walls, and exoskeleton of insects and crustaceans. Chitinases are synthesized in wide variety of organisms including plants, vertebrates, invertebrates, microbes (bacteria and fungi) and viruses. They perform various functions in different organisms depending upon the requirement of organisms like defense against pathogens and nutritional purpose. Nowadays chitinolytic enzymes have attracted global attention because of their different biotechnological and biomedical applications due to their hydrolytic activity on chitin and thus several chitinases have been reported and characterized. They are used mainly for biodegradation of chitin into beneficial compounds. These compounds have been illustrated to enhance human health through their antimicrobial, antioxidant, antitumor and anti-inflammatory properties. Chitinases have also been exploited for bio-control of phytopathogens and insects. Apart from these, the crucial use of chitinases in present time is in management of chitinous waste thus they have the potential to become essential tools in future green application. The present review focuses on the occurrence and varied distribution of chitinases. Here we also took a closer look at recent applications of chitinase in various fields.

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Section: Production Of Single Cell Proteinmentioning

confidence: 98%

Section: Production Of Single Cell Proteinmentioning

confidence: 99%

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Distribution and Biotechnological Applications of Chitinase: A Review

Dukariya¹,

Kumar²

2020

ijbb

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“…Endochitinases degrade chitin randomly at internal sites whereas exochitinases are responsible for removal of monomers or dimers of GlcNAc from the non-reducing end of chitin chains [1]. Chitinases possess a wide range of usage area such as biocontrol of fungal pathogens or insect pests, and production of single-cell proteins or ophthalmic preparations [5]. Therefore, chitinase enzymes from various organisms such as Agave tequilana [6], Eisenia fetida [7], Ostrinia furnacalis [8], and Avena chinensis [9] were studied.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of Chitinase A Gene from Serratia marcescens in Bacillus subtilis and Characterization of Enhanced Chitinolytic Activity

Okay

Alshehri

2020

Braz. arch. biol. technol.

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Chitinase enzymes possess various usages in agriculture, biotechnology and medicine due to their chitin degrading property. Thus, efficient production of chitinase enzymes with desired properties has importance for its use. In this study, chitinase A (chiA) gene from Serratia marcescens Bn10 was cloned and heterologously overexpressed using pHT43 vector in Bacillus subtilis 168. The recombinant chitinase was characterized in terms of temperature, pH, and various effectors. The extracellular chitinase activity in recombinant B. subtilis was found 2.15-fold higher than the parental strain after 2 h of IPTG induction. Optimum temperature and pH for the extracellular chitinase activity in the recombinant B. subtilis were determined as 60 o C and pH 9.0, respectively. NaCl, Ca 2+ , Mn 2+ , Cu 2+ , Zn 2+ , sodium dodecyl sulfate (SDS), Tween-20, and ethanol increased the chitinase activity whereas Mg 2+ caused an inhibition. The most notable increment on the chitinase activity was provided by Zn 2+ (3.2 folds) and then by SDS (2.9 folds). The chitinase, overproduced by the recombinant B. subtilis 168 heterologously expressing chiA, was determined to have optimum activity at high temperature and alkaline conditions as well as various effectors increase its activity. The extracellular chitinase of recombinant B. subtilis might be a promising source for agricultural, biotechnological and medical applications.

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“…Chitinases, which are capable of hydrolyzing chitin to release GlcNAc and N-acetyl chitin oligosaccharides [5], have been found in many organisms, including bacteria [6], fungi [7], plants [8], insects [9] and even humans [10]. Chitinases and chitinase-producing microorganisms have received considerable attention due to their potential applications in biological control of fungal pathogens [11] and preparation of chitin derivatives [4] in recent years.…”

Section: Introductionmentioning

confidence: 99%

A Cold-Adapted Chitinase-Producing Bacterium from Antarctica and Its Potential in Biocontrol of Plant Pathogenic Fungi

Liu

Ding

et al. 2019

Marine Drugs

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To obtain chitinase-producing microorganisms with high chitinolytic activity at low temperature, samples collected from Fildes Peninsula in Antarctica were used as sources for bioprospecting of chitinolytic microorganisms. A cold-adapted strain, designated as GWSMS-1, was isolated from marine sediment and further characterized as Pseudomonas. To improve the chitinase production, one-factor-at-a-time and orthogonal test approaches were adopted to optimize the medium components and culture conditions. The results showed that the highest chitinolytic activity (6.36 times higher than that before optimization) was obtained with 95.41 U L−1 with 15 g L−1 of glucose, 1 g L−1 of peptone, 15 g L−1 of colloid chitin and 0.25 g L−1 of magnesium ions contained in the medium, cultivated under pH 7.0 and a temperature of 20 °C. To better understand the application potential of this strain, the enzymatic properties and the antifungal activity of the crude chitinase secreted by the strain were further investigated. The crude enzyme showed the maximum catalytic activity at 35 °C and pH 4.5, and it also exhibited excellent low-temperature activity, which still displayed more than 50% of its maximal activity at 0 °C. Furthermore, the crude chitinase showed significant inhibition of fungi Verticillium dahlia CICC 2534 and Fusarium oxysporum f. sp. cucumerinum CICC 2532, which can cause cotton wilt and cucumber blight, respectively, suggesting that strain GWSMS-1 could be a competitive candidate for biological control in agriculture, especially at low temperature.

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Microbial chitinases: properties, current state and biotechnological applications

Cited by 77 publications

References 102 publications

Distribution and Biotechnological Applications of Chitinase: A Review

Distribution and Biotechnological Applications of Chitinase: A Review

Overexpression of Chitinase A Gene from Serratia marcescens in Bacillus subtilis and Characterization of Enhanced Chitinolytic Activity

A Cold-Adapted Chitinase-Producing Bacterium from Antarctica and Its Potential in Biocontrol of Plant Pathogenic Fungi

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