Immobilization and docking studies of Carlsberg subtilisin for application in poultry industry.

ABSTRACT: Carlsberg subtilisin from Bacillus licheniformis PB1 was investigated as a potential feed supplement, through immobilizing on bentonite for improving the growth rate of broilers. Initially, the pre-optimized and partially-purified protease was extracted and characterized using SDS-PAGE with MW 27.0 KDa. The MALDI-TOF-MS/MS spectrum confirmed a tryptic peptide peak with m/z 1108.496 referring to the Carlsberg subtilisin as a protein-digesting enzyme with alkaline nature. The highest free enzyme activity (30 U/mg) was observed at 50°C, 1 M potassium phosphate, and pH 8.0. the enhanced stability was observed when the enzyme was adsorbed to an inert solid support with 86.39 ± 4.36% activity retention under 20 optimized conditions. Additionally, the dried immobilized enzyme exhibited only a 5%

SUBMITTER: Rana AM 

PROVIDER: S-EPMC10431679 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature