Lignocellulose, as Earth’s most abundant renewable biomass, represents a crucial resource for the production of biofuels and biochemicals, it is of great significance for sustainable development. Microbial degradation offers a promising pathway for transforming lignocellulose into valuable products. This review explores the diversity and classification of lignocellulose-degrading microorganisms, focusing on fungi and bacteria and their respective enzyme systems responsible for breaking down cellulose, hemicellulose, and lignin. Key factors influencing degradation efficiency, including environmental conditions, substrate complexity, and microbial interactions, are thoroughly analyzed. Limitations in microbial degradation are also discussed, notably the need for identifying high-activity strains. Additionally, the review outlines future research directions, emphasizing the application of advanced technologies such as genomics, synthetic biology, and machine learning to optimize microbial degradation processes. These insights aim to enhance lignocellulose utilization efficiency, fostering its broader industrial and agricultural applications.

Ticks transmit a variety of pathogens, including rickettsia and viruses, when they feed on blood, afflicting humans and other animals. Bioactive components acting on inflammation, coagulation, and the immune system were reported to facilitate ticks’ ability to suck blood and transmit tick-borne diseases. In this study, a novel peptide, IstTx, from an Ixodes scapularis cDNA library was analyzed. The peptide IstTx, obtained by recombinant expression and purification, selectively inhibited a potassium channel, TREK-1, in a dose-dependent manner, with an IC₅₀ of 23.46 ± 0.22 μM. The peptide IstTx exhibited different characteristics from fluoxetine, and the possible interaction of the peptide IstTx binding to the channel was explored by molecular docking. Notably, extracellular acidification raised its inhibitory efficacy on the TREK-1 channel. Our results found that the tick-derived peptide IstTx blocked the TREK-1 channel and provided a novel tool acting on the potassium channel.

Due to their advantages in structural stability and versatility, cysteine-rich peptides, which are secreted from the venom glands of venomous animals, constitute a naturally occurring pharmaceutical arsenal. However, the correct folding of disulfide bonds is a challenging task in the prokaryotic expression system like Escherichia coli due to the reducing environment. Here, a secretory expression plasmid pSE-G1M5-SUMO-HWTX-I for the spider neurotoxin huwentoxin-I (HWTX-I) with three disulfides as a model of cysteine-rich peptides was constructed. By utilizing the signal peptide G1M5, the fusion protein 6 × His-SUMO-HWTX-I was successfully secreted into extracellular medium of BL21(DE3). After enrichment using cation-exchange chromatography and purification utilizing the Ni-NTA column, 6 × His-SUMO-HWTX-I was digested via Ulp1 kinase to release recombinant HWTX-I (rHWTX-I), which was further purified utilizing RP-HPLC. Finally, both impurities with low and high molecular weights were completely removed. The molecular mass of rHWTX-I was identified as being 3750.8 Da, which was identical to natural HWTX-I with three disulfide bridges. Furthermore, by utilizing whole-cell patch clamp, the sodium currents of hNa_v1.7 could be inhibited by rHWTX-I and the IC₅₀ value was 419 nmol/L.