Development and characterization of an active chitosan-based film containing quercetin

This work aims at developing an active chitosan film through the incorporation of quercetin and the evaluation of physical and functional properties of the films made thereof. The addition of quercetin showed to influence films properties in terms of surface morphology, tensile strength, and opacity while elongation-at-break, thickness, water vapor, and oxygen permeability were not significantly affected with incorporation of quercetin. The color parameters of chitosan films were affected by quercetin incorporation with a decrease of the values of L* and a*. The film exhibited a high free-radical scavenging activity, showing antioxidant activity. The film-forming solutions of chitosan with or without quercetin showed antibacterial activity against four Gram-negative and three Gram-positive bacteria. These results showed that quercetin incorporation in chitosan-based films has potential to be used as a solution for active food packaging.Author Marthyna Pessoa de Souza thanks the Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES/PDEE-Brazil) and Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE, Brazil) for fellowships. Miguel A. Cerqueira and Helder D. Silva (SFRH/BPD/72753/2010 and SFRH/BD/81288/2011, respectively) are recipients of a fellowship from the Fundacao para a Ciencia e Tecnologia (FCT, POPH-QREN and FSE Portugal). This research was financially supported by research grants and fellowships from the Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq), as well as the Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) and Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE). The authors also thank the FCT Strategic Project of UID/BIO/04469/2013 unit, the project RECI/BBB-EBI/0179/2012 (FCOMP-01-0124-FEDER-027462), and the project "BioInd - Biotechnology and Bioengineering for improved Industrial and Agro-Food processes," REF. NORTE-07-0124-FEDER-000028 Co-funded by the Programa Operacional Regional do Norte (ON. 2-O Novo Norte), QREN, FEDE

Construction of a biocompatible and antioxidant multilayer coating by layer-by-layer assembly of -carrageenan and quercetin nanoparticles

The present work aimed at the construction and characterization of a multilayer coating based on -carrageenan and quercetin-loaded lecithin/chitosan nanoparticles (Np) by the layer-by-layer technique and the evaluation of its antioxidant capacity and potential cytotoxicity in vitro. The multilayered coating was successfully self-assembled, as confirmed by UV-Vis spectroscopy, contact angle, atomic force microscopy (AFM), and scanning electron microscopy (SEM). Multilayered coatings showed to have antioxidant capacity, with a DPPH radical scavenging activity of 31.32±3.13% and a result of the FRAP assay of 799.41±95.39 M of ferrous ion (Fe2+) equivalent. These coatings were also shown to be devoid of cell toxicity, as evaluated by determination of nitric oxide production and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) test. The alveolar macrophages culture was tested in the presence of the -carrageenan/quercetin-Np multilayer coating and showed a cell viability of 91.3±9.6%. These results suggest that this multilayered coating is adequate for surfaces modification in view of biomedical and food industry applications.This work was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit, and COMPETE 2020 (POCI-01-0145-FEDER-006684) and BioTecNorte operation (NORTE01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte. The authors would also like to thank the Brazilian Government for support given by the Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq). Carneiro-daCunha, M.G. expresses her gratitude to the CNPq for research grant.info:eu-repo/semantics/publishedVersio

Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study

BACKGROUND: Haemaphysalis longicornis is a major vector of Theileria spp., Anaplasma phagocytophilum, Babesia spp. and Coxiella burnetti in East Asian countries. All life stages of ixodid ticks have a destructive pool-feeding style in which they create a pool-feeding site by lacerating host tissue and secreting a variety of biologically active compounds that allows the tick to evade host responses, enabling the uptake of a blood meal. The identification and functional characterization of tick saliva proteins can be useful to elucidate the molecular mechanisms involved in tick development and to conceive new anti-tick control methods. METHODS: H. longicornis tick saliva was collected from fully engorged nymphs and fully engorged adults induced by dopamine or pilocarpine, respectively. Saliva was digested with trypsin for LC-MS/MS sequencing and peptides were searched against tick and rabbit sequences. RESULTS: A total of 275 proteins were identified, of which 135 were tick and 100 were rabbit proteins. Of the tick proteins, 30 proteins were identified exclusively in fully engorged nymph saliva, 74 in fully engorged adult females, and 31 were detected in both stages. The identified tick proteins include heme/iron metabolism-related proteins, oxidation/detoxification proteins, enzymes, proteinase inhibitors, tick-specific protein families, and cytoskeletal proteins. Proteins involved in signal transduction, transport and metabolism of carbohydrate, energy, nucleotide, amino acids and lipids were also detected. Of the rabbit proteins, 13 were present in nymph saliva, 48 in adult saliva, and 30 were present in both. The host proteins include immunoglobulins, complement system proteins, antimicrobial proteins, serum albumin, peroxiredoxin, serotransferrin, apolipoprotein, hemopexin, proteinase inhibitors, and hemoglobin/red blood cells-related products. CONCLUSIONS: This study allows the identification of H. longicornis saliva proteins. In spontaneously detached tick saliva various proteins were identified, although results obtained with saliva of fully engorged ticks need to be carefully interpreted. However, it is interesting to note that proteins identified in this study were also described in other tick saliva proteomes using partially engorged tick saliva, including hemelipoprotein, proteases, protease inhibitors, proteins related to structural functions, transporter activity, metabolic processes, and others. In conclusion, these data can provide a deeper understanding to the biology of H. longicornis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13071-015-0918-y) contains supplementary material, which is available to authorized users

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship

Effect of an edible nanomultilayer coating by electrostatic self-assembly on the shelf life of fresh-cut mangoes

This work aims at evaluating the effect of an alginate-chitosan nanomultilayer coating, obtained by electrostatic layer-by-layer self-assembling, in the quality and shelf life of fresh-cut mangoes. Coated and uncoated fresh-cut mangoes were stored under refrigeration (8 °C) for 14 days. The changes in mass loss, titratable acidity, pH, ascorbic acid content, total soluble solids, malondialdehyde content, browning rate, and microbial count were evaluated during storage. At the end of the storage period, lower values of mass loss, pH, malondialdehyde content, browning rate, soluble solids, microorganisms proliferation, and higher titratable acidity were observed in the coated mangoes. The nanomultilayer coating did not improve the retention of vitamin C during storage of fresh-cut mangoes. Results suggest that chitosan-alginate nanomultilayer edible coating extends the shelf life of fresh-cut mangoes up to 8 days.Author Marthyna Pessoa de Souza thanks Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES/PDEE-Brazil) and Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE, Brazil) for granting her scholarships. The authors thank the Fundacao para a Ciencia e a Tecnologia (FCT) Strategic Project PEst-OE/EQB/LA0023/2013 and the Project "BioInd-Biotechnology and Bioengineering for improved Industrial and Agro-Food processes", REF. NORTE-07-0124-FEDER-000028, co-funded by the Programa Operacional Regional do Norte (ON.2-O Novo Norte), QREN, and FEDER (Portugal)