Improved Mannan-degrading Enzymes' Production by Aspergillus Niger Through Medium Optimization
Overview
Biotechnology
Molecular Biology
Affiliations
The effect of different carbon and nitrogen sources on the production of mannan-degrading enzymes, focussing on β-mannanase, by Aspergillus niger was investigated using shake flask culture. The β-mannanase activity obtained during growth of A. niger on guar gum (GG, 1495 nkat mL(-1)) was much higher than those observed on other carbon substrates, locust bean gum (1148 nkat mL(-1)), α-cellulose (10.7 nkat mL(-1)), glucose (8.8 nkat mL(-1)) and carboxymethylcellulose (4.6 nkat mL(-1)). For fermentation using GG as a carbon source, bacteriological peptone gave the highest β-mannanase activity (1744 nkat mL(-1)) followed by peptone from meat (1168 nkat mL(-1)), yeast extract (817 nkat mL(-1)), ammonium sulphate (241 nkat mL(-1)), ammonium nitrate (113 nkat mL(-1)) and ammonium chloride (99 nkat mL(-1)) when used as a nitrogen source. The composition of bacteriological peptone and initial pH of the medium were further optimized using response surface methodology (RSM). Medium consisted of 21.3 g L(-1) GG and 57 g L(-1) peptone with initial culture pH of 5.5 was optimum for β-mannanase production (2063 nkat mL(-1)) by A. niger. The β-mannanase production obtained in this study using A. niger was significantly higher than those reported in the literature.
Nath S, Kango N Sci Rep. 2024; 14(1):14015.
PMID: 38890382 PMC: 11637063. DOI: 10.1038/s41598-024-63803-4.
Applications of Microbial β-Mannanases.
Dawood A, Ma K Front Bioeng Biotechnol. 2021; 8:598630.
PMID: 33384989 PMC: 7770148. DOI: 10.3389/fbioe.2020.598630.
Enhancement of -Mannanase Production by ATCC11774 through Optimization of Medium Composition.
Norizan N, Halim M, Tan J, Abbasiliasi S, Mat Sahri M, Othman F Molecules. 2020; 25(15).
PMID: 32752106 PMC: 7435724. DOI: 10.3390/molecules25153516.
Ahirwar S, Soni H, Rawat H, Prajapati B, Kango N Mycology. 2018; 7(3):143-153.
PMID: 30123626 PMC: 6059128. DOI: 10.1080/21501203.2016.1229697.