El-Borai et al., A. (2022). Enhancement of β-1,3-1,4-Glucanase Production by Marine halomonas meridiana ES021 via Statistical Optimization and Cell Immobilization. Egyptian Journal of Aquatic Biology and Fisheries, 26(6), 781-802. doi: 10.21608/ejabf.2022.276391
Aliaa M. El-Borai et al.. "Enhancement of β-1,3-1,4-Glucanase Production by Marine halomonas meridiana ES021 via Statistical Optimization and Cell Immobilization". Egyptian Journal of Aquatic Biology and Fisheries, 26, 6, 2022, 781-802. doi: 10.21608/ejabf.2022.276391
El-Borai et al., A. (2022). 'Enhancement of β-1,3-1,4-Glucanase Production by Marine halomonas meridiana ES021 via Statistical Optimization and Cell Immobilization', Egyptian Journal of Aquatic Biology and Fisheries, 26(6), pp. 781-802. doi: 10.21608/ejabf.2022.276391
El-Borai et al., A. Enhancement of β-1,3-1,4-Glucanase Production by Marine halomonas meridiana ES021 via Statistical Optimization and Cell Immobilization. Egyptian Journal of Aquatic Biology and Fisheries, 2022; 26(6): 781-802. doi: 10.21608/ejabf.2022.276391
Enhancement of β-1,3-1,4-Glucanase Production by Marine halomonas meridiana ES021 via Statistical Optimization and Cell Immobilization
β-1,3-1,4-glucanase (β-glucanase) is an enzybiotic enzyme that cleaves linear β-glucans with β-1,3 and β-1,4 linkage, including cereal β-glucans. It has several applications in industry, agriculture, and medicine in which it has been observed with a broad antimicrobial spectrum. A local marine strain with high activity of β-glucanase was screened and isolated from Gabal El-Zeit offshore in the Red Sea of Egypt. It was successfully identified through a partially 16S rRNA gene sequencing technique as Halomonas meridiana ES021. The medium was optimized using a multifactorial matrix of Plackett-Burman design, and the most influencing components were barley flour, urea and KH2PO4. The enzyme activity was positively affected by barley flour, urea and negatively affected by KH2PO4. The optimal medium obtained through statistical design increased enzyme activity by 1.4-fold from 455.83±20.45 to 597.50±24.50U/ mL. In addition, a Box-Behnken experimental design was studied to investigate interactions between barley flour, urea and KH2PO4 concentrations. In the optimized medium, the enzyme activity was increased by about 1.8-fold from 597.50±24.50 U/mL to 1095.50±31.00 U/mL. Moreover, cell immobilization by adsorption and entrapment was investigated and immobilized cultures of Halomonas meridiana ES021, which were entrapped in a 3% agarose gel produced the maximal β-glucanase activity, which was about 1111.67 ± 29U/ mL, followed by cultures adsorbed on clay particles, which was about 916.97 ±29.47U/ mL.
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