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Characterization of Bioactive Components in Edible Algae

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ISBN: 9783039285600 / 9783039285617 Year: Pages: 226 DOI: 10.3390/books978-3-03928-561-7 Language: eng
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology --- Nutrition and Food Sciences
Added to DOAB on : 2020-06-09 16:38:57
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Algae have been used since ancient times as food for humans, animal feed, agricultural fertilizer, and as a source of substances for therapeutic use. Currently, seaweed represents a vast source of raw materials used in the pharmaceutical, food, traditional medicine, and cosmetics industries. They are nutritionally valuable, both fresh and dried, or as ingredients in a wide variety of pre-made foods. In particular, seaweed contains significant amounts of protein, lipids, minerals, and vitamins. Information is limited on the role of algae and their metabolites in therapy. Only a few taxa have been studied for use in medicine. Many traditional cultures report the healing powers of selected algae in tropical and subtropical marine forms. This is especially true in the maritime areas of Asia, where the sea plays a significant role in daily activities. However, currently, only a few genera and species of algae are involved in aspects of medicine and therapy. The beneficial uses of seaweed or seaweed products include those that can mimic specific manifestations of human disease, production of antibiotic compounds, or improved human nutrition.

Plant Proteomic Research 2.0

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ISBN: 9783039210626 9783039210633 Year: Pages: 594 DOI: 10.3390/books978-3-03921-063-3 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology --- Plant Sciences
Added to DOAB on : 2019-06-26 08:44:07
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Advancements in high-throughput “Omics” techniques have revolutionized plant molecular biology research. Proteomics offers one of the best options for the functional analysis of translated regions of the genome, generating a wealth of detailed information regarding the intrinsic mechanisms of plant stress responses. Various proteomic approaches are being exploited extensively for elucidating master regulator proteins which play key roles in stress perception and signaling, and these approaches largely involve gel-based and gel-free techniques, including both label-based and label-free protein quantification. Furthermore, post-translational modifications, subcellular localization, and protein–protein interactions provide deeper insight into protein molecular function. Their diverse applications contribute to the revelation of new insights into plant molecular responses to various biotic and abiotic stressors.

Keywords

Phalaenopsis --- petal --- pollination --- senescence --- 2-DE --- ROS --- Medicago sativa --- leaf cell wall proteome --- cadmium --- quantitative proteomics --- 2D DIGE --- chloroplast --- elevated CO2 --- heat stress --- nucleotide pyrophosphatase/phosphodiesterase --- (phospho)-proteomics --- photosynthesis --- protein phosphorylation --- 14-3-3 proteins --- Oryza sativa L. --- starch --- sucrose --- N utilization efficiency --- proteomics --- 2D --- protein phosphatase --- rice isogenic line --- SnRK1 --- 14-3-3 --- lettuce --- bolting --- proteome --- high temperature --- iTRAQ --- proteome profiling --- iTRAQ --- differentially abundant proteins (DAPs) --- drought stress --- physiological responses --- Zea mays L. --- GS3 --- ? subunit --- heterotrimeric G protein --- mass spectrometric analysis --- RGG3 --- rice --- western blotting --- Dn1-1 --- ?-subunit --- heterotrimeric G protein --- mass spectrometry analysis --- RGG4 --- rice --- western blotting --- Clematis terniflora DC. --- polyphenol oxidase --- virus induced gene silencing --- photosynthesis --- glycolysis --- Camellia sinensis --- chlorotic mutation --- chlorophyll deficiency --- weakening of carbon metabolism --- iTRAQ --- proteomics --- degradome --- wheat --- cultivar --- protease --- papain-like cysteine protease (PLCP) --- subtilase --- metacaspase --- caspase-like --- wheat leaf rust --- Puccinia recondita --- Stagonospora nodorum --- iTRAQ --- proteomics --- somatic embryogenesis --- pyruvate biosynthesis --- Zea mays --- chlorophylls --- LC-MS-based proteomics --- pea (Pisum sativum L.) --- proteome functional annotation --- proteome map --- seeds --- seed proteomics --- late blight disease --- potato proteomics --- Phytophthora infestans --- Sarpo Mira --- early and late disease stages --- Simmondsia chinensis --- cold stress --- proteomics --- leaf --- iTRAQ --- Ricinus communis L. --- cold stress --- seed imbibition --- iTRAQ --- proteomics --- Morus --- organ --- gel-free/label-free proteomics --- flavonoid --- antioxidant activity --- phosphoproteome --- barley --- seed dormancy --- germination --- imbibition --- after-ripening --- sugarcane --- Sporisorium scitamineum --- smut --- proteomics --- RT-qPCR --- ISR --- holm oak --- Quercus ilex --- 2-DE proteomics --- shotgun proteomics --- non-orthodox seed --- population variability --- stresses responses --- ammonium --- Arabidopsis thaliana --- carbon metabolism --- nitrogen metabolism --- nitrate --- proteomics --- root --- secondary metabolism --- proteomics --- wheat --- silver nanoparticles --- plant pathogenesis responses --- data-independent acquisition --- quantitative proteomics --- Pseudomonas syringae --- sweet potato plants infected by SPFMV --- SPV2 and SPVG --- sweet potato plants non-infected by SPFMV --- SPV2 and SPVG --- co-infection --- transcriptome profiling --- gene ontology --- pathway analysis --- lesion mimic mutant --- leaf spot --- phenylpropanoid biosynthesis --- proteomics --- isobaric tags for relative and absolute quantitation (iTRAQ) --- rice --- affinity chromatography --- ergosterol --- fungal perception --- innate immunity --- pattern recognition receptors --- plasma membrane --- proteomics --- proteomics --- maize --- plant-derived smoke --- shoot --- Solanum tuberosum --- patatin --- seed storage proteins --- vegetative storage proteins --- tuber phosphoproteome --- targeted two-dimensional electrophoresis --- B. acuminata petals --- MALDI-TOF/TOF --- GC-TOF-MS --- qRT-PCR --- differential proteins --- n/a

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