The diversity of lignin-degrading bacteria in Qinling Mountain is revealed. The study of Burkholderia sp. H1 expands the range of bacteria for lignin degradation and provides novel bacteria for application to lignocellulosic biomass.
Lignin valorization can be obtained through cleavage of selected bonds by microbial enzymes, in which lignin is segregated from cellulose and hemicellulose and abundant phenolic compounds can be provided. In this study, Pseudomonas sp. Q18, previously isolated from rotten wood in China, was used to degrade alkali lignin and raw lignocellulosic material. Gel-permeation chromatography, field-emission scanning electron microscope, and GC-MS were combined to investigate the degradation process. The GC-MS results revealed that the quantities of aromatic compounds with phenol ring from lignin increased significantly after incubation with Pseudomonas sp. Q18, which indicated the degradation of lignin. According to the lignin-derived metabolite analysis, it was proposed that a DyP-type peroxidase (PmDyP) might exist in strain Q18. Thereafter, the gene of PmDyP was cloned and expressed, after which the recombinant PmDyP was purified and the enzymatic kinetics of PmDyP were assayed. According to results, PmDyP showed promising characteristics for lignocellulosic biodegradation in biorefinery.
Cell wall degrading enzymes break down the cell wall by degrading the main cell wall components and destroying structure of the cell wall without influencing the protein. Effects of various enzymes (Viscozyme® L, cellulase, hemicellulase, and pectinase) on the molecular weight distribution of peanut protein and yield of peanut protein and oil bodies during an aqueous enzymatic extraction process were investigated in this study. The molecular weight distribution of peanut protein was not changed, and Viscozyme® L was selected to assist peanut protein and oil bodies extraction by the aqueous extraction process. The aqueous enzymatic extraction process was optimized by a signal factor experiment and response surface methodology, and the optimal condition was enzyme hydrolysis temperature of 52°C, solid-liquid ratio of 1 : 4, enzyme concentration of 1.35%, and enzyme hydrolysis time of 90 min. A peanut protein yield of 78.60% and oil bodies yield of 48.44% were achieved under the optimal condition. Compared with commercial peanut protein powder (CPPP), the solubility and foaming properties of peanut protein powder obtained by aqueous enzymatic extraction (AEEPPP) were a little lower. However, the functional properties of foam stability, emulsifying activity, emulsifying stability, water holding capacity, and oil holding capacity of AEEPPP were better than that of CPPP.
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