Chitosanase Production from the Liquid Fermentation of Squid Pens Waste by Paenibacillus elgii .

Autor: Doan CT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Tran TN; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Tran TPH; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen TT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen HK; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Tran TKT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Vu BT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Trinh THT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen AD; Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Wang SL; Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan.; Life Science Development Center, Tamkang University, New Taipei City 25137, Taiwan.
Jazyk: angličtina
Zdroj: Polymers [Polymers (Basel)] 2023 Sep 11; Vol. 15 (18). Date of Electronic Publication: 2023 Sep 11.
DOI: 10.3390/polym15183724
Abstrakt: Chitosanases play a significant part in the hydrolysis of chitosan to form chitooligosaccharides (COS) that possess diverse biological activities. This study aimed to enhance the productivity of Paenibacillus elgii TKU051 chitosanase by fermentation from chitinous fishery wastes. The ideal parameters for achieving maximum chitosanase activity were determined: a squid pens powder amount of 5.278% ( w / v ), an initial pH value of 8.93, an incubation temperature of 38 °C, and an incubation duration of 5.73 days. The resulting chitosanase activity of the culture medium was 2.023 U/mL. A chitosanase with a molecular weight of 25 kDa was isolated from the culture medium of P. elgii TKU051 and was biochemically characterized. Liquid chromatography with tandem mass spectrometry analysis revealed that P. elgii TKU051 chitosanase exhibited a maximum amino acid identity of 43% with a chitosanase of Bacillus circulans belonging to the glycoside hydrolase (GH) family 46. P. elgii TKU051 chitosanase demonstrated optimal activity at pH 5.5 while displaying remarkable stability within the pH range of 5.0 to 9.0. The enzyme displayed maximum efficiency at 60 °C and demonstrated considerable stability at temperatures ≤40 °C. The presence of Mn 2+ positively affected the activity of the enzyme, while the presence of Cu 2+ had a negative effect. Thin-layer chromatography analysis demonstrated that P. elgii TKU051 chitosanase exhibited an endo-type cleavage pattern and hydrolyzed chitosan with 98% degree of deacetylation to yield (GlcN) 2 and (GlcN) 3 . The enzymatic properties of P. elgii TKU051 chitosanase render it a promising candidate for application in the production of COS.
Databáze: MEDLINE
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