Study of nano-hydroxyapatite tagged alkaline protease isolated from Himalayan sub-alpine Forest soil bacteria and role in recalcitrant feather waste degradation

• Published in: International journal of biological macromolecules 2023-12, Vol.253, p.127317-127317, Article 127317
• Main Authors: Sengupta, Shritoma, Basak, Pijush, Ghosh, Piya, Pramanik, Arnab, Chakraborty, Aparna, Mukhopadhyay, Mainak, Sen, Aparna, Bhattacharyya, Maitree
• Format: Article
• Language: English
• Subjects: calcium; Calcium hydroxyapatite nanoparticles; enzyme activity; forest soils; metalloproteinases; Recalcitrant solid waste degradation; serine; Serine metalloprotease; Stenotrophomonas maltophilia; Sub-alpine forest soil; temperature; thermal stability; value added; wastes
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2023.127317

Purified calcium serine metalloprotease from Stenotrophomonas maltophilia strain SMPB12 exhibits highest enzyme activity at pH 9 and temperature range between 15 °C–25 °C. Enzyme supplemented with 40 μM Ca-Hap-NP (NP-protease) showed maximum elevated activity of 17.29 μmole/min/ml (1.9-fold of original protease activity). The thermostability of the enzyme was maintained for 1 h at 60 °C over an alkaline pH range 7.5–10, as compared to the NP untreated enzyme whose activity was of 8.97 μmole/min/ml. A significant loss of activity with EDTA (1.05 μmole/min/ml, 11.75 %), PMSF (0.93 μmole/min/ml, 10.46 %) and Hg2+ (3.81 μmole/min/ml, 42.49 %) was also observed. Kinetics study of NP-protease showed maximum decreases in Km (28.11 %) from 0.28 mM (NP untreated enzyme) to 0.22 mM (NP-protease) along with maximum increase in Vmax (42.88 %) from 1.25 μmole/min/ml to 1.79 μmole/min/ml at varying temperatures. The enhanced activity of NP-protease was able to efficiently degrade recalcitrant solid wastes like feather to produce value-added products like amino acids and helps in declogging recalcitrant solid wastes. The nano-enabled protease may be utilized in a smaller amount for degrading in bulk recalcitrant solid proteinaceous waste at 15 °C temperature as declogging agents providing an eco-friendly efficient process. •Psychrotrophic bacteria S. maltophilia SMPB12 isolated from subalpine forest soil•Minimalistic growth media for high protease production•Serine metalloprotease showing tolerance against wide range of substances•Showing high proteolytic activity in degrading feather•Enhanced enzyme activity with Ca-Hap-NP for recalcitrant solid waste degradation