11.2% of school dropouts had severe and extreme grades of depression as against 3% among school going and nil among college going adolescents.
This work was aimed at immobilization, characterization, and utilization of chitinase from Kurthia gibsonii Mb126. Immobilization of Kurthia gibsonii Mb126 chitinase on glutaraldehyde treated chitosan was carried out with immobilization yield of 106%. The optimal factors of the immobilization technique such as concentration of glutaraldehyde, chitinase concentration, and immobilization time were evaluated. After optimizing process parameters of immobilization (Glutaraldehyde concentration 4%, chitinase conc. 60mg, immobilization time 30min.), the specific activity of immobilized chitinase improved to 4.3-fold compared to the free form of chitinase. Temperature and pH optima of the immobilized chitinase and free enzyme were same i.e., 7.5 and 40°C respectively. The relative activity of immobilized chitinase remained 90% at 40°C, at 50°C, and at 60°C for 120 min. In the pH range from 5.5 to 8, the immobilized chitinase retained 100% activity. The results confirmed that the pH stability and thermal stability of chitinase increased by immobilizing chitinase on chitosan. The immobilized enzyme system maintained 90% of its efficiency even after 16 successive reaction cycles. The immobilized chitinase maintained 78% of its activity even after 20 months. Fermentation of prawn shell waste with immobilized chitinase indicated a high level of deproteinization. Deproteinization experiments were carried out with 5mL (0.4 mg/mL ) of immobilized and free chitinase on 300 mg/mL of prawn shell waste for 20 days without any additional supplements at 40°C and 6.5 pH. Protein content was reduced from 38.4 to 0.8% with immobilized chitinase. Results suggests the possibility of using immobilized enzymes to remove the prawn shell waste from the environment. To the best of our knowledge there was no such study about the deproteinization of prawn shell waste using immobilized chitinase till the date.
The main dengue and Zika vector, Aedes aegypti, is a cosmotropic species. Since dengue fever cases have significantly increased in recent years, these organisms seem to be extremely detrimental. Synthetic pesticides are not biodegradable, are non-selective, and have adverse effects on beneficial organisms being handled in the vector management system. In the present study, the mosquitocidal potential of chitinase from P. putida Mb 12 was evaluated in an effort to identify risk-free options for the control of mosquitoes. Larvicidal toxicity of Pseudomonas putida Mb 12 chitinase were evaluated on IVth-instar larva of Ae. aegypti and their effect on acetylcholinesterase activity and glutathione S-transferase activity were studied. The early 4th instar larvae of Ae. aegypti were exposed to chitinase enzyme concentrations of 50U/mL, 100U/mL, 200U/mL, and 500U/mL for a period of 4 hours to assess their effectiveness. The results showed that as chitinase concentration increased, mosquito larvae mortality increased; after 4 hours, chitinase at 500 U/mL caused 100% mortality. After 4 hours of incubation, 200 U/mL was administered to achieve LC50 (which kills 50% of the exposed organisms), and after 3 hours, 500 U/mL was used to obtain LC90 values. During the study, it was discovered that different quantities of chitinase (100 U/mL, 200 U/mL, and 500 U/mL) inhibited 80% of the activity of the acetylcholinesterase enzyme. This study found that chitinase significantly increased glutathione S-transferase activity. Additionally, it was discovered that the chitinase treatment was non-hazardous to guppy fish. It was assumed that the P. putida Mb 12 chitinase tested was safe to employ in the aquatic habitat because no mortality was observed in the non-target organisms.
Background of the study: As fungi become resistant to commonly used pesticides, fungicides are becoming not only more expensive, but also less effective in controlling postharvest infections. New chitinase immobilisation techniques are urgently needed to minimize enzyme costs while enhancing bio catalytic performance, antifungal activity, enzyme stability, and reusability. Objectives: The objective of this study was to immobilise chitinase of Kurthia gibsonii Mb126 by entrapping it in calcium alginate beads and to analyse its antifungal activities against Aspergillus flavus. Methods: The optimal parameters influencing the immobilization process and the characteristics of soluble and immobilised chitinase of K. gibsonii Mb126 were analysed. The antifungal activities of immobilised and free chitinase of K. gibsonii Mb126 against A. flavus, which was isolated from decayed lemon fruit, were performed using the agar-disk diffusion method. Free chitinase 25.0 mL (0.8 U/mL) and immobilised chitinase 0.06 g (specific activity 124-192 U/mg) were treated on separate lemon fruits for testing antifungal activity against A. flavus. Findings: K. gibsonii Mb126 chitinase was immobilised perfectly in calcium alginate beads. After optimising process parameters of immobilisation (sodium alginate concentration 3%, calcium chloride 0.2 M, 120 min. curing time), the specific activity of K. gibsonii Mb126 immobilised chitinase improved to 11.9-fold greater than the free form of chitinase and the immobilisation yield increased to 84%. It was observed that the thermal stability and storage stability of immobilised chitinase were better than those of free enzymes. The immobilised chitinase could be reused, and it retained 78% activity even after 16 cycles. The surface morphology of immobilised chitinase was observed in a scanning electron microscope at different magnification powers. Enzyme kinetics was studied and compared with that of its chitinase soluble counterpart. An in vitro study demonstrated that immobilised chitinase of K. gibsonii Mb126 has higher antifungal activity against A. flavus. In vivo experimental study of the https://www.indjst.org/ 136
Our target is to evaluate recent literature on chitinase production from different sources via solid-state fermentation and to analyze several strategies to improve chitinase production via solid-state fermentation. Plant pathogen biocontrol, sequential transformation of chitin into bioactive molecules such as chito-oligosaccharides and N-acetylglucosamine, protoplast synthesis from filamentous fungi, and single-cell protein production are some of the applications for chitinase. Despite their enormous biological importance, chitinases have received little commercial importance due to the smaller percentage of microbes with high efficiencies, the enzymes' decreased activity and consistency, and the cost of production. Solid-state fermentation (SSF) is less expensive, requires fewer vessels, uses less water, requires fewer wastewater treatments, produces a greater product yield, has a lower risk of bacterial contamination, and requires less energy expenditure. Despite its higher productivity and lower cost, the SSF technique is now mostly limited to lab scales. Furthermore, the crude SSF products can be used as an enzyme source for biotransformation. There are many findings on different microorganisms that produce chitinase by SSF. So it is very critical to isolate new organisms for such production. So we assessed the traditional approach to medium optimization, which focuses on changing one factor at a time while leaving the others constant, and statistical optimization techniques such as response surface methodology (RSM), artificial neural networks (ANNs), and genetic algorithms (GA).
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