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.
Kurthia gibsonii Mb126, Chitinase, Deproteinization, immobilization, chitosan
Share This Article
© The Author(s) 2022. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.