Marine-derived biowaste was valorized to develop chitin/fish gelatin porous materials with the aim of being used as moisture scavengers and bioactive carriers. Chitin was extracted from squid pens, abundant and available biowastes from fishery industry, through a sustainable process and the environmental assessment was carried out. Besides the valorization of biowaste, it is worth noting that the use of this specific biowaste allows the avoidance of discoloration and demineralization processes to extract chitin and, thus, a lower consumption of resources, both chemicals and energy, in comparison to the conventional chitin extraction from crustacean shells. Consequently, this alternative source of chitin brings economic and environmental benefits. In addition to the reduction of food waste disposal, the incorporation of squid pen-extracted chitin into fish gelatin formulations led to the conversion of a biowaste into a value-added product. In this regard, chitin was employed as a reinforcing agent in order to improve the mechanical behavior of fish gelatin materials. It is worth noting that good compatibility between gelatin and chitin was achieved since no chitin aggregation was observed. Furthermore, more defined pores were obtained after chitin addition. Additionally, tetrahydrocurcumin was incorporated into the formulation as a bioactive and its release was analyzed during three days. It was observed that samples prepared with chitin and THC showed potential as active porous materials for bioactive delivery.
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http://dx.doi.org/10.1016/j.scitotenv.2019.135747 | DOI Listing |
Pest Manag Sci
January 2025
Dpto. Microbiología, Facultad de Ciencias, Universidad de Málaga, Málaga, Spain.
Background: Chitin is a crucial component of fungal cell walls and an effective elicitor of plant immunity; however, phytopathogenic fungi have developed virulence mechanisms to counteract the activation of this plant defensive response. In this study, the molecular mechanism of chitin-induced suppression through effectors involved in chitin deacetylases (CDAs) and their degradation (EWCAs) was investigated with the idea of developing novel dsRNA-biofungicides to control the cucurbit powdery mildew caused by Podosphaera xanthii.
Results: The molecular mechanisms associated with the silencing effect of the PxCDA and PxEWCAs genes were first studied through dsRNA cotyledon infiltration assays, which revealed a ≈80% reduction in fungal biomass and a 50% decrease in gene expression.
Int J Mol Sci
December 2024
Liaoning Engineering and Technology Research Center for Insect Resources, College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang 110866, China.
Chitin deacetylases (CDAs) are carbohydrate esterases associated with chitin metabolism and the conversion of chitin into chitosan. Studies have demonstrated that chitin deacetylation is essential for chitin organization and compactness and therefore influences the mechanical and permeability properties of chitinous structures, such as the peritrophic membrane (PM) and cuticle. In the present study, two genes ( and ) encoding CDA protein isoforms were identified and characterized in Chinese oak silkworm () larvae.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Plant Breeding and Acclimatization Institute-National Research Institute, Radzikow, 05-870 Blonie, Poland.
Int J Mol Sci
December 2024
Department of Neurology, Davis School of Medicine, University of California, 1515 Newton Court, Davis, CA 95618, USA.
We have designed and produced 39 amino acid peptide mimics of the and human acetylcholine receptors' (AChRs) main immunogenic regions (MIRs). These conformationally sensitive regions consist of three non-contiguous segments of the AChR α-subunits and are the target of 50-70% of the anti-AChR autoantibodies (Abs) in human myasthenic serum and in the serum of rats with a model of that disease, experimental autoimmune myasthenia gravis (EAMG), induced by immunizing the rats with the electric organ AChR. These MIR segments covalently joined together bind a significant fraction of the monoclonal antibodies (mAbs) raised in rats against electric organ AChR.
View Article and Find Full Text PDFMolecules
December 2024
Department of Chemistry and Life Science, Kogakuin University, Tokyo 192-0015, Japan.
YKL-40 is structurally similar to chitotriosidase (CHIT1), an active chitinase, but it lacks chitin-degrading activity while retaining chitin-binding capability. Elevated YKL-40 levels are associated with inflammatory diseases and cancers, making it a valuable biomarker. We previously reported that the W69T substitution in YKL-40 significantly reduces its chitin-binding affinity, identifying W69 as a crucial binding site.
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