淡江大學機構典藏:Item 987654321/121293
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    Title: Production of thermophilic chitinase by Paenibacillus sp. TKU052 by bioprocessing of chitinous fishery wastes and its application in N-acetyl-D-glucosamine production
    Authors: CT, Doan;TN, Tran;SL, Wang
    Keywords: chitinous fishery wastes;chitinase;crab shells;Paenibacillus;N-acetyl-D-glucosamine
    Date: 2021-09-09
    Issue Date: 2021-09-13 12:10:19 (UTC+8)
    Publisher: MDPI
    Abstract: The bioprocessing of chitinous fishery wastes (CFWs) to chitinases through fermentation
    approaches has gained importance owing to its great benefits in reducing the enzyme production
    cost, and utilizing chitin waste. In this work, our study of the chitinase production of Paenibacillus sp.
    TKU052 in the presence of different kinds of CFWs revealed a preference for demineralized crab
    shells powder (deCSP); furthermore, a 72 kDa chitinase was isolated from the 0.5% deCSP-containing
    medium. The Paenibacillus sp. TKU052 chitinase displayed maximum activity at 70 ◦C and pH 4–5,
    while Zn2+, Fe3+, Triton X-100, Tween 40, and SDS exerted a negative effect on its activity, whereas
    Mn2+ and 2-mercaptoethanol were found to potentially enhance the activity. Among various kinds
    of polysaccharide, Paenibacillus sp. TKU052 chitinase exhibited the best catalytic activity on colloidal
    chitin (CC) with Km = 9.75 mg/mL and Vmax = 2.43 µmol/min. The assessment of the hydrolysis of
    CC and N-acetyl chitooligosaccharides revealed that Paenibacillus sp. TKU052 chitinase possesses multiple catalytic functions, including exochitinase, endochitinase, and N-acetyl-β-D-glucosaminidase
    activities. Finally, the combination of Paenibacillus sp. TKU052 chitinase and Streptomyces speibonae
    TKU048 N-acetyl-β-D-glucosaminidase could efficiently convert CC to N-acetyl-D-glucosamine
    (GlcNAc) with a production yield of 94.35–98.60% in 12–24 h.
    Relation: Polymers 13(18), 3048
    DOI: 10.3390/polym13183048
    Appears in Collections:[化學學系暨研究所] 期刊論文

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