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      Bioactivity and biochemical efficacy of chitinase and Justicia brandegeana extract against Red Palm Weevil Rhynchophorus ferrugineus Olivier (Coleoptera: Curculionidae)

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          Abstract

          The red palm weevil Rhynchophorus ferrugineus is a large polyphagous insect, and this study was carried out to isolate chitinase from Beauveria bassiana as well as phytochemical screening of Justicia brandegeana to elucidate its effect as biocontrol agents against the red palm weevil and its possible effect on enzymatic bioactivity. It is the first time that the lipoid constituents of J. brandegeana were examined by both gas–liquid chromatography (GLC) and gas chromatography–mass spectrometry (GC/Mass). The results showed that the highest rates of mortality in treated prepupae were 35.0% and 30.0% with the higher concentration of chitinase (25 ppm) and petroleum ether extract of J. brandegeana (1,200 ppm), respectively. Moreover, changes in enzyme activity of ALP, PO, GPT, and GOT in the prepupal stage after treatment with LC 50 chitinase and J. brandegeana extract were 36.63 & 14.32, −21.99 & 41.20, −11.02 & 47.05, and −36.00 & 21.43% compared with untreated control, respectively. This study demonstrated effectiveness of chitinase, and the petroleum ether extract of J. brandegeana has potent effect against Rh. ferrugineus due to its disturbance effect on the enzymatic system, protein as well as DNA damage.

          Abstract

          Chitinase was extracted from Beauveria bassiana and Phytochemical screening of Justicia brandegeana was performed to elucidate its effect as biocontrol agents against Rhynchophorus ferrugineus and its possible effect on enzymatic bioactivity of ALP, PO, GPT, and GOT as well as on DNA and protein content. This study demonstrated effectiveness of chitinase, and the petroleum ether extract of J. brandegeana has potent effect against Rh. ferrugineus due to its disturbance effect on the enzymatic system, protein as well as DNA damage.

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          Most cited references38

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          The prophenoloxidase-activating system in invertebrates.

          A major innate defense system in invertebrates is the melanization of pathogens and damaged tissues. This important process is controlled by the enzyme phenoloxidase (PO) that in turn is regulated in a highly elaborate manner for avoiding unnecessary production of highly toxic and reactive compounds. Recent progress, especially in arthropods, in the elucidation of mechanisms controlling the activation of zymogenic proPO into active PO by a cascade of serine proteinases and other factors is reviewed. The proPO-activating system (proPO system) is triggered by the presence of minute amounts of compounds of microbial origins, such as beta-1,3-glucans, lipopolysaccharides, and peptidoglycans, which ensures that the system will become active in the presence of potential pathogens. The presence of specific proteinase inhibitors prevents superfluous activation. Concomitant with proPO activation, many other immune reactions will be produced, such as the generation of factors with anti-microbial, cytotoxic, opsonic, or encapsulation-promoting activities.
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            Role of the prophenoloxidase-activating system in invertebrate immunity.

            The melanization reaction, which is a common response to parasite entry in invertebrate animals, especially arthropods, is due to the activity of an oxidoreductase, phenoloxidase. This enzyme is part of a complex system of proteinases, pattern recognition proteins and proteinase inhibitors constituting the so-called prophenoloxidase-activating system. It is proposed to be a non-self recognition system because conversion of prophenoloxidase to active enzyme can be brought about by minuscule amounts of molecules such as lipopolysaccharide, peptidoglycan and beta-1, 3-glucans from micro-organisms. Several components of this system recently have been isolated and their structure determined.
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              Research Applications of Proteolytic Enzymes in Molecular Biology

              Proteolytic enzymes (also termed peptidases, proteases and proteinases) are capable of hydrolyzing peptide bonds in proteins. They can be found in all living organisms, from viruses to animals and humans. Proteolytic enzymes have great medical and pharmaceutical importance due to their key role in biological processes and in the life-cycle of many pathogens. Proteases are extensively applied enzymes in several sectors of industry and biotechnology, furthermore, numerous research applications require their use, including production of Klenow fragments, peptide synthesis, digestion of unwanted proteins during nucleic acid purification, cell culturing and tissue dissociation, preparation of recombinant antibody fragments for research, diagnostics and therapy, exploration of the structure-function relationships by structural studies, removal of affinity tags from fusion proteins in recombinant protein techniques, peptide sequencing and proteolytic digestion of proteins in proteomics. The aim of this paper is to review the molecular biological aspects of proteolytic enzymes and summarize their applications in the life sciences.
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                Author and article information

                Contributors
                aashehawy@uqu.edu.sa
                shqari@uqu.edu.sa
                Journal
                Food Sci Nutr
                Food Sci Nutr
                10.1002/(ISSN)2048-7177
                FSN3
                Food Science & Nutrition
                John Wiley and Sons Inc. (Hoboken )
                2048-7177
                16 July 2020
                August 2020
                : 8
                : 8 ( doiID: 10.1002/fsn3.v8.8 )
                : 4625-4636
                Affiliations
                [ 1 ] Biology Department Aljumum University College Umm Al‐Qura University Makkah Saudi Arabia
                [ 2 ] Plant Protection Research Institute Agricultural Research Centre Giza Egypt
                [ 3 ] Pharmacognosy Department Faculty of Pharmacy Sinai University Cairo Egypt
                [ 4 ] Pharmacognosy Department Faculty of Pharmacy Al‐Azhar University Cairo Egypt
                Author notes
                [*] [* ] Correspondence

                Ayman A. Shehawy and Sameer H. Qari, Biology Department, Aljumum University College, Umm Al‐Qura University, Makkah, Saudi Arabia.

                Emails: aashehawy@ 123456uqu.edu.sa (A. A. S.); shqari@ 123456uqu.edu.sa (S. H. Q.)

                Author information
                https://orcid.org/0000-0003-2463-8466
                https://orcid.org/0000-0001-9424-5217
                Article
                FSN31787
                10.1002/fsn3.1787
                7455953
                060b05bf-d054-4086-a8ff-52b5730c641f
                © 2020 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC.

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 15 June 2020
                : 27 June 2020
                : 30 June 2020
                Page count
                Figures: 4, Tables: 7, Pages: 12, Words: 8160
                Funding
                Funded by: Umm Al‐Qura University , open-funder-registry 10.13039/501100006701;
                Award ID: 18‐SCI‐1‐01‐0005
                Categories
                Original Research
                Original Research
                Custom metadata
                2.0
                August 2020
                Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.8 mode:remove_FC converted:29.08.2020

                biochemical,chitinase,justicia brandegeana,red palm weevil

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