Structural, Physicochemical and Functional Properties of Protein Extracted from De-Oiled Field Muskmelon (Cucumis melo L. var. agrestis Naud.) Seed Cake.

For oil plants, the oil extraction method is a crucial factor in influencing the functional characteristics of the protein. However, reports of protein functionality as affected by the oil extraction process are scarce. In this study, field muskmelon seed (FMS) protein was extracted by Soxhlet extraction method (SE), organic solvent extraction method (OSE), aqueous extraction method (AE), and pressing extraction method (PE), and its structure, amino acid profile, physicochemical properties, and functionality were determined. Molecular weight distribution was similar for all FMS proteins, whereas protein aggregates contents were most excellent for SE and OSE. FMS protein comprised predominantly glutamic acid, leucine, aspartic acid, arginine, and proline. Total amino acids content was highest for SE. Differences in functionality between four FMS proteins for different oil extraction methods were vast. PE had the highest value of solubility, and AE exhibited the lowest. AE had the greatest water and oil holding capacity. PE presented better foaming and emulsion capacities than other samples. This study demonstrated that the extraction oil method could impact the protein's physicochemical and associated functional characteristics. High-quality plant oil and protein could be simultaneously obtained by modulating the oil extraction method in future research.

Precise Antibody-Independent m6A Identification via 4SedTTP-Involved and FTO-Assisted Strategy at Single-Nucleotide Resolution.

Innovative detection techniques to achieve precise m6A distribution within mammalian transcriptome can advance our understanding of its biological functions. We specifically introduced the atom-specific replacement of oxygen with progressively larger atoms (sulfur and selenium) at 4-position of deoxythymidine triphosphate to weaken its ability to base pair with m6A, while maintaining A-T* base pair virtually the same as the natural one. 4SedTTP turned out to be an outstanding candidate that endowed m6A with a specific signature of RT truncation, thereby making this "RT-silent" modification detectable with the assistance of m6A demethylase FTO through next-generation sequencing. This antibody-independent, 4SedTTP-involved and FTO-assisted strategy is applicable in m6A identification, even for two closely gathered m6A sites, within an unknown region at single-nucleotide resolution.