11,12 Chitinases have potential applications in various areas of biotechnology, biomedicine, agriculture, and nutrition. 10 Bacterial chitinases have a size range of 20–60 kDa. 3 Most chitin-degrading prokaryotes are the gliding bacteria, pseudomonad, vibrio, enterobacteria, actinomycete, bacilli, and clostridia. 9 Chitinase participates in a variety of functions, including defense, nutrient digestion, morphogenesis, and pathogenesis. 5,7,8Ĭhitinases (EC 3.2.1.14) are present in a wide range of organisms, including viruses, bacteria, fungi, insects, higher plants, and animals these enzymes are capable of catalyzing the hydrolysis of chitin. 6 Therefore, organisms that produce chitin-degrading enzymes can be useful in bioremediation and waste management as well as help release nutrients and maintain the carbon, nitrogen, and other biogeochemical cycles in the environment. 5 These wastes may pose as an environmental threat on their accumulation and due to extremely slow decomposition. 4 Chitinous wastes are also produced in large amounts in industries such as seafood processing industry, which produces prawn waste (containing 23% chitin). 3 This natural resource is relatively easily accessible, e.g., from sources such as shrimp, crab, and krill, which are considered as waste chitin accounts for 20–58% of the dry weight of these wastes. 1,2 Several million tons of chitin is synthesized and degraded each year in the biosphere. In addition, the study of the morphological alteration of chitin treated by enzyme by SEM revealed cracks and pores on the chitin surface, indicating a potential application of this enzyme in several industries.Ĭhitin, a β-1,4 polymer of N-acetyl- d-glucosamine (GlcNAc), which is widely distributed among fungi, crustaceans, molluscs, coelenterates, protozoan, and green algae, is the second-most abundant biopolymer found in nature after cellulose. Ag +, Co 2+, iodoacetamide, and iodoacetic acid inhibited the enzyme activity, whereas Mn 2+, Cu 2+, Tweens (20 and 80), Triton X-100, and EDTA increased the same. From the tested values, the best pH/temperature was obtained at pH 5 and 70 ☌, with K m and V max values of chitinase to be 5.6 mg/mL and 0.87 μmol/min, respectively. Our results demonstrated that inoculation amount and temperature of incubation were the most significant factors influencing chitinase production. The colloidal chitin, peptone, and K 2HPO 4 represented the best carbon, nitrogen, and phosphorus sources, respectively. A01 in the suitable liquid medium resulted in the production of high levels of enzyme. A01 based on 16S rDNA sequencing and by matching the key morphological, physiological, and biochemical characteristics. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. Determination of michaelis and rate constant.
Selection of carbon, nitrogen, and phosphorus sources.Pcr amplification and study of 16s rrna gene.Screening of thermophilic chitinase-producing microorganism.
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