Find in Library

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 <i>Paenibacillus</i> 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 <i>Paenibacillus</i> 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, <i>Paenibacillus</i> sp. TKU052 chitinase exhibited the best catalytic activity on colloidal chitin (CC) with K<i>_m</i> = 9.75 mg/mL and V<i>_max</i> = 2.43 μmol/min. The assessment of the hydrolysis of CC and <i>N</i>-acetyl chitooligosaccharides revealed that <i>Paenibacillus</i> sp. TKU052 chitinase possesses multiple catalytic functions, including exochitinase, endochitinase, and <i>N</i>-acetyl-β-D-glucosaminidase activities. Finally, the combination of <i>Paenibacillus</i> sp. TKU052 chitinase and <i>Streptomyces speibonae</i> TKU048 <i>N</i>-acetyl-β-D-glucosaminidase could efficiently convert CC to <i>N</i>-acetyl-D-glucosamine (GlcNAc) with a production yield of 94.35–98.60% in 12–24 h.