ABSTRACT
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of recalcitrant polysaccharides. There are limited reports on LPMOs capable of concurrently catalyzing the oxidative cleavage of both cellulose and chitin. In this study, we identified and cloned a novel LPMO from the newly isolated bacterium Chitinilyticum aquatile CSC-1, designated as CaLPMO10. When using 2, 6-dimethylphenol (2, 6-DMP) as the substrate, CaLPMO10 exhibited optimal activity at 50 °C and pH 8, demonstrating good temperature stability at 30 °C. Even after a 6 h incubation at pH 8 and 30 °C, CaLPMO10 retained approximately 83.03 ± 1.25% residual enzyme activity. Most metal ions were found to enhance the enzyme activity of CaLPMO10, with ascorbic acid identified as the optimal reducing agent. Mass spectrometry analysis indicated that CaLPMO10 displayed oxidative activity towards both chitin and cellulose, identifying it as a C1/C4-oxidized LPMO. CaLPMO10 shows promise as a key enzyme for the efficient utilization of biomass resources in future applications.
ABSTRACT
To develop a high-efficient extraction method, we investigated the use of high-pressure homogenization (HPH) as a novel pretreatment technology for the extraction of sodium alginate (SA) from Laminaria japonica. After the single-factor experiment, the results demonstrated that under the conditions of 100 MPa HPH pressure, 4 cycles, pH 6.0, and 0.5% EDTA for 3.0 h, the optimized extraction yield of HPH reached 34%. To further clarify the effect on the structural properties of HPH-extracted SA, we conducted comprehensive analysis using SEM, FTIR, MRS, NMR, XRD, TGA, and a T-AOC assay. Our findings revealed that HPH pretreatment significantly disrupted the structure of L. japonica cells and reduced their crystallinity to 76.27%. Furthermore, the antioxidant activity of HPH-extracted SA reached 0.02942 mgVceqâmg-1. Therefore, the HPH pretreatment method is a potential strategy for the extraction of alginate.
