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The application of carbon fiber-reinforced composite materials in marine engineering is growing steadily. The mechanical properties of unbonded flexible risers using composite tensile armor wire are highly valued. However, the curing process generates a certain amount of internal residual stress. We present a detailed analysis of epoxy resin laminates to assess the impact of thermal, chemical, and mechanical effects on the curing stress and strain. An empirical model that correlates temperature and degree of cure was developed to precisely fit the elastic modulus data of the curing resin. The chemical kinetics of the epoxy resin system was characterized using differential scanning calorimetry (DSC), while the tensile relaxation modulus was determined through a dynamic mechanical analysis. The viscoelastic model was calibrated using the elastic modulus data of the cured resin combining temperature and degree of the curing (thermochemical kinetics) responses. Based on the principle of time–temperature superposition, the displacement factor and relaxation behavior of the material were also accurately captured by employing the same principle of time–temperature superposition. Utilizing the empirical model for degree of cure and modulus, we predicted micro-curing-induced strains in cured composite materials, which were then validated with experimental observations.

Fusarium wilt caused by Fusarium oxysporum f. sp. lentis (Fol) is the most devastating disease of lentil present worldwide. Identification of multi-race fusarium wilt resistance genes and their incorporation into existing cultivars will help to reduce yield losses. In the present study, 100 lentil germplasms belonging to seven lentil species were screened against seven prevalent races of Fol, and accessions IC201561 (Lens culinaris subsp. culinaris), EC714243 (L. c. subsp. odemensis), and EC718238 (L. nigricans) were identified as resistant. The typical R gene codes for the nucleotide-binding site and leucine-rich repeats (NBS-LRR) at the C terminal are linked to either the Toll/interleukin 1-like receptor (TIR) or coiled coil (CC) at the N terminal. In the present study, degenerate primers, designed from the NBS region amplifying the P-loop to the GLPLA motif, isolated forty-five resistance gene analogues (RGAs) from identified resistant accessions. The sequence alignment identified both classes of RGAs, TIR and non-TIR, based on the presence of aspartate (D) and tryptophan (W) at the end of the kinase motif, respectively. The phylogenetic analysis grouped the RGAs into six classes, from LRGA1 to LRGA6, which determined the diversity of the RGAs present in the host. Grouping of the RGAs identified from Lens nigricans, LnRGA 2, 9, 13 with I2 revealed the structural similarity with the fusarium resistance gene. The similarity index ranged from 27.85% to 86.98% among the RGAs and from 26.83% to 49.41% among the known R genes, I2, Gpa2, M, and L6. The active binding sites present along the conserved motifs grouped the RGAs into 13 groups. ADP/ATP, being the potential ligand, determines the ATP binding and ATP hydrolysis activity of the RGAs. The isolated RGAs can be used to develop markers linked to the functional R gene. Furthermore, expression analysis and full-length gene isolation pave the path to identifying the molecular mechanism involved in resistance.

In this paper, the authors introduce the notion of weak r-level LM-G-filter spaces and strong p-level LM-G-filter spaces and discuss certain properties of these spaces. The study identifies [Formula: see text]-G, the category of weak r-level LM-G-filter spaces as an isomorphism-closed bireflective full subcategory of LM-G, the category of LM-G-filter spaces. It is also proved that [Formula: see text]-G, the category of strong p-level LM-G-filter spaces is an isomorphism-closed bicoreflective full subcategory of LM-G. Moreover, level decompositions of LM-G-filter spaces are studied and some properties of the associated L-pre G-filter spaces are obtained.

In this study, albumin, globulin, and glutelin were extracted from white finger millet, and their amino acid content, functional and structural properties were investigated. The protein concentration of albumin, globulin, and glutelin were 76.01%, 74.32%, and 69.55%, respectively. The results showed that all the fractions had a significant amount of essential amino acids. Aqueous protein dispersions (10%, w/v) were treated for 12 min at different ultrasound power levels (100, 200, and 300 W). The solubility, emulsifying, and foaming properties of albumin and glutelin were significantly (p < 0.05) improved after ultrasound treatment (20 kHz) which indicates that ultrasound could unfold protein aggregates. A decrease in particle size, increase in surface hydrophobicity, and zeta potential correlated with improved functional properties. Ultrasound treatment reduced the size of all proteins except for fractions at 300 W and also sodium dodecyl sulfate–polyacrylamide gel electrophoresis revealed a significant change in the molecular weight of albumin and glutelin at 300 W. Scanning electron microscopy of treated protein fraction showed distinctive microstructure with irregular structure compared to untreated protein fraction. Although Fourier transform infrared spectroscopy spectra of proteins were similar after ultrasonication, a partial increase in the intensity of the Amide A band was observed. In conclusion, the ultrasound‐treated protein fraction can be used as a high‐value plant‐based emulsifier. [ABSTRACT FROM AUTHOR]