{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T23:14:02Z","timestamp":1790896442769,"version":"4.1.0"},"reference-count":118,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2022,8,28]],"date-time":"2022-08-28T00:00:00Z","timestamp":1661644800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Russian Foundation for Basic Research","award":["19-416-390001"],"award-info":[{"award-number":["19-416-390001"]}]},{"name":"Russian Foundation for Basic Research","award":["14-s\/2021"],"award-info":[{"award-number":["14-s\/2021"]}]},{"name":"Government of the Kaliningrad Region","award":["19-416-390001"],"award-info":[{"award-number":["19-416-390001"]}]},{"name":"Government of the Kaliningrad Region","award":["14-s\/2021"],"award-info":[{"award-number":["14-s\/2021"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Dextran, a renewable hydrophilic polysaccharide, is nontoxic, highly stable but intrinsically biodegradable. The \u03b1-1, 6 glycosidic bonds in dextran are attacked by dextranase (E.C. 3.2.1.11) which is an inducible enzyme. Dextranase finds many applications such as, in sugar industry, in the production of human plasma substitutes, and for the treatment and prevention of dental plaque. Currently, dextranases are obtained from terrestrial fungi which have longer duration for production but not very tolerant to environmental conditions and have safety concerns. Marine bacteria have been proposed as an alternative source of these enzymes and can provide prospects to overcome these issues. Indeed, marine bacterial dextranases are reportedly more effective and suitable for dental caries prevention and treatment. Here, we focused on properties of dextran, properties of dextran\u2014hydrolyzing enzymes, particularly from marine sources and the biochemical features of these enzymes. Lastly the potential use of these marine bacterial dextranase to remove dental plaque has been discussed. The review covers dextranase-producing bacteria isolated from shrimp, fish, algae, sea slit, and sea water, as well as from macro- and micro fungi and other microorganisms. It is common knowledge that dextranase is used in the sugar industry; produced as a result of hydrolysis by dextranase and have prebiotic properties which influence the consistency and texture of food products. In medicine, dextranases are used to make blood substitutes. In addition, dextranase is used to produce low molecular weight dextran and cytotoxic dextran. Furthermore, dextranase is used to enhance antibiotic activity in endocarditis. It has been established that dextranase from marine bacteria is the most preferable for removing plaque, as it has a high enzymatic activity. This study lays the groundwork for the future design and development of different oral care products, based on enzymes derived from marine bacteria.<\/jats:p>","DOI":"10.3390\/molecules27175533","type":"journal-article","created":{"date-parts":[[2022,8,29]],"date-time":"2022-08-29T22:53:42Z","timestamp":1661813622000},"page":"5533","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Marine Bacterial Dextranases: Fundamentals and Applications"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9694-9138","authenticated-orcid":false,"given":"Noora","family":"Barzkar","sequence":"first","affiliation":[{"name":"Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, Bandar Abbas 74576, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4921-8997","authenticated-orcid":false,"given":"Olga","family":"Babich","sequence":"additional","affiliation":[{"name":"Institute of Living Systems, Immanuel Kant Baltic Federal University, 236016 Kaliningrad, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rakesh","family":"Das","sequence":"additional","affiliation":[{"name":"Department of Paraclinical Sciences, Faculty of Veterinary Medicine, Norwegian University of Life Sciences (NMBU), 1432 \u00c5s, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stanislav","family":"Sukhikh","sequence":"additional","affiliation":[{"name":"Institute of Living Systems, Immanuel Kant Baltic Federal University, 236016 Kaliningrad, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9245-8745","authenticated-orcid":false,"given":"Saeid","family":"Tamadoni Jahromi","sequence":"additional","affiliation":[{"name":"Persian Gulf and Oman Sea Ecology Research Center, Iranian Fisheries Sciences Research Institute, Agricultural Research Education and Extension Organization (AREEO), Bandar Abbas 14578, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7208-9441","authenticated-orcid":false,"given":"Muhammad","family":"Sohail","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Karachi, Karachi 75270, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,8,28]]},"reference":[{"key":"ref_1","unstructured":"Du Boil, P.M., and Wienese, S. (2002). Enzymic Reduction of Dextran in Process-Laboratory Evaluation of Dextranases, Citeseer."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/j.carbpol.2012.01.030","article-title":"Enzymatically degradable nanoparticles of dextran esters as potential drug delivery systems","volume":"88","author":"Kaewprapan","year":"2012","journal-title":"Carbohydr. Polym."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1007\/s10295-016-1886-8","article-title":"Purification, characterization, and application of a thermostable dextranase from Talaromyces pinophilus","volume":"44","author":"Zhang","year":"2017","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1128\/MMBR.69.2.306-325.2005","article-title":"Microbial dextran-hydrolyzing enzymes: Fundamentals and applications","volume":"69","author":"Khalikova","year":"2005","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_5","first-page":"61","article-title":"Impact of sugarcane delivery schedule on product value at raw sugar factories","volume":"22","author":"Salassi","year":"2004","journal-title":"J. Agribus."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1021\/jf00014a012","article-title":"Specific method for quantitative measurement of the total dextran content of raw sugar","volume":"40","author":"Brown","year":"1992","journal-title":"J. Agric. Food Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/s12355-009-0020-x","article-title":"Application of dextranases in sugarcane factory: Overcoming practical problems","volume":"11","author":"Eggleston","year":"2009","journal-title":"Sugar Tech"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Eggleston, G., Dilks, A., Blowers, M., and Winters, K. (2011, January 2\u20135). Successful Application of Dextranase in Sugar Beet Factories. Proceedings of the American Society of Sugarbeet Technologists Meeting, Albuquerque, NM, USA.","DOI":"10.5274\/ASSBT.2011.59"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/j.jbiotec.2007.07.946","article-title":"Immobilization of dextranase from Chaetomium erraticum","volume":"131","author":"Erhardt","year":"2007","journal-title":"J. Biotechnol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0032-9592(02)00058-4","article-title":"Degradation of dental plaque glucans and prevention of glucan formation using commercial enzymes","volume":"38","author":"Marotta","year":"2002","journal-title":"Process Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1007\/s11274-010-0558-5","article-title":"Functional oligosaccharides: Production, properties and applications","volume":"27","author":"Patel","year":"2011","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s12355-010-0026-4","article-title":"Dextranase production from Paecilomyces lilacinus and its application for dextran removal from sugarcane juice","volume":"12","author":"Bhatia","year":"2010","journal-title":"Sugar Tech"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1111\/j.1348-0421.2004.tb03501.x","article-title":"Molecular characterization of dextranase from Streptococcus rattus","volume":"48","author":"Igarashi","year":"2004","journal-title":"Microbiol. Immunol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0032-9592(98)00127-7","article-title":"Preparation and some properties of immobilized Penicillium funiculosum 258 dextranase","volume":"34","author":"Ismail","year":"1999","journal-title":"Process Biochem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1155\/2012\/860619","article-title":"Characterization of extracellular dextranase from a novel halophilic Bacillus subtilis NRC-B233b a mutagenic honey isolate under solid state fermentation","volume":"9","author":"Esawy","year":"2012","journal-title":"J. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.jchromb.2003.08.037","article-title":"Purification and properties of extracellular dextranase from a Bacillus sp.","volume":"796","author":"Khalikova","year":"2003","journal-title":"J. Chromatogr. B"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1080\/01490451.2019.1605427","article-title":"Degradation of long chain polymer (Dextran) using thermostable dextranase from hydrothermal spring isolate (Bacillus megaterium)","volume":"36","author":"Shahid","year":"2019","journal-title":"Geomicrobiol. J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.ijbiomac.2015.04.007","article-title":"Purification, characterization and end product analysis of dextran degrading endodextranase from Bacillus licheniformis KIBGE-IB25","volume":"78","author":"Zohra","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_19","first-page":"1934578X20953286","article-title":"Isomalto-oligosaccharides produced by endodextranase Shewanella sp. GZ-7 from sugarcane plants","volume":"15","author":"Liu","year":"2020","journal-title":"Nat. Prod. Commun."},{"key":"ref_20","first-page":"331","article-title":"Crystal structure of thermophilic dextranase from Thermoanaerobacter pseudethanolicus","volume":"159","author":"Suzuki","year":"2016","journal-title":"J. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1007\/s10068-010-0106-y","article-title":"Biochemical characterization of dextranase from Arthrobacter oxydans and its cloning and expression in Escherichia coli","volume":"19","author":"Lee","year":"2010","journal-title":"Food Sci. Biotechnol."},{"key":"ref_22","first-page":"205","article-title":"Studies on dextran-degrading enzymes. Isolation and identification of a dextranase-producing strain of Cytophaga johnsonii and studies on the formation of the surface-bound enzyme","volume":"88","author":"Janson","year":"1975","journal-title":"Microbiology"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"19927","DOI":"10.1074\/jbc.M111.339036","article-title":"Novel dextranase catalyzing cycloisomaltooligosaccharide formation and identification of catalytic amino acids and their functions using chemical rescue approach","volume":"287","author":"Kim","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"6581","DOI":"10.1007\/s00253-019-09965-y","article-title":"A novel intracellular dextranase derived from Paenibacillus sp. 598K with an ability to degrade cycloisomaltooligosaccharides","volume":"103","author":"Mizushima","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1007\/s00253-007-0936-6","article-title":"A Paenibacillus sp. dextranase mutant pool with improved thermostability and activity","volume":"75","author":"Hild","year":"2007","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0008-6215(00)84814-4","article-title":"Purification and substrate specificity of an endo-dextranase of Streptococcus mutans K1-R","volume":"54","author":"Pulkownik","year":"1977","journal-title":"Carbohydr. Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1007\/s12355-015-0378-x","article-title":"Kinetic and thermodynamic properties of partially purified dextranase from Paecilomyces lilacinus and its application in dextran removal from cane juice","volume":"18","author":"Bhatia","year":"2016","journal-title":"Sugar Tech"},{"key":"ref_28","first-page":"1095","article-title":"Microbial production and characterization of dextranase","volume":"3","author":"Mahmoud","year":"2014","journal-title":"Int. J. Curr. Microbiol. App. Sci."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Huang, R., Zhong, L., Xie, F., Wei, L., Gan, L., Wang, X., and Liao, A. (2019). Purification, characterization and degradation performance of a novel dextranase from Penicillium cyclopium CICC-4022. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20061360"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1016\/j.procbio.2011.06.025","article-title":"Purification and characterization of extracellular dextranase from a novel producer, Hypocrea lixii F1002, and its use in oligodextran production","volume":"46","author":"Wu","year":"2011","journal-title":"Process Biochem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1590\/0001-3765201820160333","article-title":"Statistical tools application on dextranase production from Pochonia chlamydosporia (VC4) and its application on dextran removal from sugarcane juice","volume":"90","author":"Sufiate","year":"2018","journal-title":"An. Da Acad. Bras. De Ci\u00eanc."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.molcatb.2015.08.020","article-title":"Kinetics and thermodynamic of the purified dextranase from Chaetomium erraticum","volume":"122","year":"2015","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/s12355-018-0652-9","article-title":"Purification and characterization including dextran hydrolysis of dextranase from Aspergillus allahabadii X26","volume":"21","author":"Netsopa","year":"2019","journal-title":"Sugar Tech"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/s10295-013-1369-0","article-title":"Characterization of a marine-derived dextranase and its application to the prevention of dental caries","volume":"41","author":"Jiao","year":"2014","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1002\/jobm.202100310","article-title":"Alkalic dextranase produced by marine bacterium Cellulosimicrobium sp. PX02 and its application","volume":"61","author":"Ning","year":"2021","journal-title":"J. Basic Microbiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1007\/s00343-015-4376-3","article-title":"Optimization of four types of antimicrobial agents to increase the inhibitory ability of marine Arthrobacter oxydans KQ11 dextranase mouthwash","volume":"34","author":"Ren","year":"2016","journal-title":"Chin. J. Oceanol. Limnol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"4355","DOI":"10.1021\/acs.jafc.9b01290","article-title":"Crystal structure of GH49 dextranase from Arthrobacter oxidans KQ11: Identification of catalytic base and improvement of thermostability using semirational design based on B-factors","volume":"67","author":"Ren","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1007\/s13205-013-0187-4","article-title":"Application of statistical design for the optimization of dextranase production by a novel fungus isolated from Red Sea sponge","volume":"4","author":"Abdelwahed","year":"2014","journal-title":"3 Biotech"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/s00253-009-2121-6","article-title":"Characterization of novel thermostable dextranase from Thermotoga lettingae TMO","volume":"85","author":"Kim","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"637","DOI":"10.4014\/jmb.1112.12024","article-title":"Biochemical characterization of thermophilic dextranase from a thermophilic bacterium, Thermoanaerobacter pseudethanolicus","volume":"22","author":"Park","year":"2012","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"657","DOI":"10.2174\/1389203711109070657","article-title":"Molecular determinants of enzyme cold adaptation: Comparative structural and computational studies of cold-and warm-adapted enzymes","volume":"12","author":"Papaleo","year":"2011","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.pep.2004.09.002","article-title":"Cloning, expression, and purification of a recombinant cold-adapted \u03b2-galactosidase from Antarctic bacterium Pseudoalteromonas sp. 22b","volume":"39","author":"Kur","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"ref_43","first-page":"278","article-title":"The pH of various tooth-whitening products on the South African market: Scientific","volume":"66","author":"Majeed","year":"2011","journal-title":"S. Afr. Dent. J."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1093\/ps\/84.7.998","article-title":"Isomaltooligosaccharide increases cecal Bifidobacterium population in young broiler chickens","volume":"84","author":"Thitaram","year":"2005","journal-title":"Poult. Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1016\/S0969-2126(03)00147-3","article-title":"Dextranase from Penicillium minioluteum: Reaction course, crystal structure, and product complex","volume":"11","author":"Larsson","year":"2003","journal-title":"Structure"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1016\/j.carres.2004.05.031","article-title":"The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases","volume":"339","author":"Hayacibara","year":"2004","journal-title":"Carbohydr. Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/0141-0229(94)90058-2","article-title":"A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides","volume":"16","author":"Kim","year":"1994","journal-title":"Enzym. Microb. Technol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/BF02984375","article-title":"Designing Instruction for Attitudinal Outcomes","volume":"2","author":"Simonson","year":"1979","journal-title":"J. Instr. Dev."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1042\/bj3230757","article-title":"Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger A.T.C.C. 9642","volume":"323","author":"Aoki","year":"1997","journal-title":"Biochem. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0195-6663(03)00045-X","article-title":"Veganism as status passage: The process of becoming a vegan among youths in Sweden","volume":"41","author":"Larsson","year":"2003","journal-title":"Appetite"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1007\/s002940000119","article-title":"Carbon source regulation of a dextranase gene from the filamentous fungus Penicillium minioluteum","volume":"37","year":"2000","journal-title":"Curr. Genet."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1006\/bbrc.2001.4316","article-title":"Molecular cloning of an \u03b1-glucosidase-like gene from Penicillium minioluteum and structure prediction of its gene product","volume":"281","author":"Castellanos","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","unstructured":"Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) (1965). Enzyme Nomenclature: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes, Academic Press."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"91","DOI":"10.4052\/tigg.15.91","article-title":"Production of cyclodextran and its application","volume":"15","author":"Oguma","year":"2003","journal-title":"Trends Glycosci. Glycotechnol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1007\/s002849900092","article-title":"Extracellular \u03b1-glucosidase with dextran-hydrolyzing activity from the thermophilic fungus, Thermomyces lanuginosus","volume":"33","author":"Jensen","year":"1996","journal-title":"Curr. Microbiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1042\/bj2800309","article-title":"A classification of glycosyl hydrolases based on amino acid sequence similarities","volume":"280","author":"Henrissat","year":"1991","journal-title":"Biochem. J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1104\/pp.124.4.1515","article-title":"Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics","volume":"124","author":"Henrissat","year":"2000","journal-title":"Plant Physiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1042\/bj3230859","article-title":"A classification of dextran-hydrolysing enzymes based on amino-acid-sequence similarities","volume":"323","author":"Aoki","year":"1997","journal-title":"Biochem. J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0959-440X(00)00253-0","article-title":"Glycoside hydrolases and glycosyltransferases: Families and functional modules","volume":"11","author":"Bourne","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/449403a","article-title":"Ocean pipes could help the Earth to cure itself","volume":"449","author":"Lovelock","year":"2007","journal-title":"Nature"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/S1359-6446(03)02713-2","article-title":"Drugs from the deep: Marine natural products as drug candidates","volume":"8","author":"Haefner","year":"2003","journal-title":"Drug Discov. Today"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"18907","DOI":"10.1007\/s11356-017-9379-5","article-title":"Proximate composition and mineral contents in the body wall of two species of sea cucumber from Oman Sea","volume":"24","author":"Barzkar","year":"2017","journal-title":"Environ. Sci. Pollut. Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"736376","DOI":"10.1016\/j.aquaculture.2021.736376","article-title":"Corrigendum to \u201cEffect of different levels of dietary Sargassum cristaefolium on growth performance, hematological parameters, histological structure of hepatopancreas and intestinal microbiota of Litopenaeus vannamei\u201d","volume":"535","author":"Jahromi","year":"2021","journal-title":"Aquaculture"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1016\/j.ijbiomac.2020.06.072","article-title":"Marine microbial alkaline protease: An efficient and essential tool for various industrial applications","volume":"161","author":"Barzkar","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/s00792-018-1009-8","article-title":"Thermostable marine microbial proteases for industrial applications: Scopes and risks","volume":"22","author":"Barzkar","year":"2018","journal-title":"Extremophiles"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Barzkar, N., Jahromi, S.T., Poorsaheli, H.B., and Vianello, F. (2019). Metabolites from marine microorganisms, micro, and macroalgae: Immense scope for pharmacology. Mar. Drugs, 17.","DOI":"10.3390\/md17080464"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Barzkar, N., Jahromi, S.T., and Vianello, F. (2022). Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity. Mar. Drugs, 20.","DOI":"10.3390\/md20010046"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.ijbiomac.2020.12.134","article-title":"A critical review on marine serine protease and its inhibitors: A new wave of drugs?","volume":"170","author":"Barzkar","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"6873","DOI":"10.1007\/s00253-020-10692-y","article-title":"An overview on marine cellulolytic enzymes and their potential applications","volume":"104","author":"Barzkar","year":"2020","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1007\/s12010-020-03483-8","article-title":"Marine bacterial esterases: Emerging biocatalysts for industrial applications","volume":"193","author":"Barzkar","year":"2021","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4453","DOI":"10.1007\/s00253-021-11356-1","article-title":"Marine microbial L-glutaminase: From pharmaceutical to food industry","volume":"105","author":"Barzkar","year":"2021","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.micro.57.030502.091022","article-title":"The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides","volume":"58","author":"Bayer","year":"2004","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1016\/j.ijbiomac.2018.09.083","article-title":"Marine bacterial chitinase as sources of energy, eco-friendly agent, and industrial biocatalyst","volume":"120","author":"Jahromi","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"6847","DOI":"10.1007\/s00253-018-9156-5","article-title":"Future direction in marine bacterial agarases for industrial applications","volume":"102","author":"Jahromi","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Barzkar, N., Sheng, R., Sohail, M., Jahromi, S.T., Babich, O., Sukhikh, S., and Nahavandi, R. (2022). Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future. Molecules, 27.","DOI":"10.3390\/molecules27113375"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Lai, X., Liu, X., Liu, X., Deng, T., Feng, Y., Tian, X., Lyu, M., and Wang, S. (2019). The marine Catenovulum agarivorans MNH15 and dextranase: Removing dental plaque. Mar. Drugs, 17.","DOI":"10.3390\/md17100592"},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Ren, W., Cai, R., Yan, W., Lyu, M., Fang, Y., and Wang, S. (2018). Purification and characterization of a biofilm-degradable dextranase from a marine bacterium. Mar. Drugs, 16.","DOI":"10.3390\/md16020051"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s13213-013-0644-7","article-title":"Screening, production, and characterization of dextranase from Catenovulum sp.","volume":"64","author":"Cai","year":"2014","journal-title":"Ann. Microbiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"105678","DOI":"10.1016\/j.pep.2020.105678","article-title":"Expression, purification and characterization of a cold-adapted dextranase from marine bacteria and its ability to remove dental plaque","volume":"174","author":"Deng","year":"2020","journal-title":"Protein Expr. Purif."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Liu, H., Ren, W., Ly, M., Li, H., and Wang, S. (2019). Characterization of an alkaline GH49 dextranase from marine bacterium Arthrobacter oxydans KQ11 and its application in the preparation of isomalto-oligosaccharide. Mar. Drugs, 17.","DOI":"10.3390\/md17080479"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1080\/08927014.2016.1239722","article-title":"Dextranase from Arthrobacter oxydans KQ11-1 inhibits biofilm formation by polysaccharide hydrolysis","volume":"32","author":"Wang","year":"2016","journal-title":"Biofouling"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.ijbiomac.2014.07.006","article-title":"The atmospheric and room-temperature plasma (ARTP) method on the dextranase activity and structure","volume":"70","author":"Wang","year":"2014","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.carbpol.2014.01.102","article-title":"Purification and characterization of a novel marine Arthrobacter oxydans KQ11 dextranase","volume":"106","author":"Wang","year":"2014","journal-title":"Carbohydr. Polym."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"fnab007","DOI":"10.1093\/femsle\/fnab007","article-title":"A novel dextranase gene from the marine bacterium Bacillus aquimaris S5 and its expression and characteristics","volume":"368","author":"Dong","year":"2021","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"7423","DOI":"10.1128\/jb.173.23.7423-7428.1991","article-title":"Molecular cloning of the extracellular endodextranase of Streptococcus salivarius","volume":"173","author":"Lawman","year":"1991","journal-title":"J. Bacteriol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"813079","DOI":"10.3389\/fbioe.2021.813079","article-title":"Purification, Characterization, and Hydrolysate Analysis of Dextranase From Arthrobacter oxydans G6-4B","volume":"9","author":"Liu","year":"2022","journal-title":"Front. Bioeng. Biotechnol."},{"key":"ref_87","first-page":"167","article-title":"In Vitro and In Silico Characterization of a Novel Dextranase from Pochonia Chlamydosporia","volume":"8","author":"Sufiate","year":"2018","journal-title":"Biotech"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1080\/15422119.2017.1279628","article-title":"Recent Advances in Protein Extraction Using Ionic Liquid-Based Aqueous Two-Phase Systems","volume":"46","author":"Lee","year":"2017","journal-title":"Sep. Purif. Rev."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.bej.2018.04.002","article-title":"Improving Cell Disruption Efficiency to Facilitate Protein Release from Microalgae Using Chemical and Mechanical Integrated Method","volume":"135","author":"Phong","year":"2018","journal-title":"Biochem. Eng. J."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"e2000797","DOI":"10.1002\/cbdv.202000797","article-title":"Food-Grade Expression and Characterization of a Dextranase from Chaetomium Gracile Suitable for Sugarcane Juice Clarification","volume":"18","author":"Zhao","year":"2021","journal-title":"Chem. Biodivers."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.bbrc.2019.12.010","article-title":"Enzymatic Synthesis of Non-Digestible Oligosaccharide Catalyzed by Dextransucrase and Dextranase from Maltose Acceptor Reaction","volume":"523","author":"Huang","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4375","DOI":"10.1128\/iai.61.10.4375-4381.1993","article-title":"Expression and secretion of an Arthrobacter dextranase in the oral bacterium Streptococcus gordonii","volume":"61","author":"Kubo","year":"1993","journal-title":"Infect. Immun."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Juntarachot, N., Kantachote, D., Peerajan, S., Sirilun, S., and Chaiyasut, C. (2020). Optimization of fungal dextranase production and its antibiofilm activity, encapsulation and stability in toothpaste. Molecules, 25.","DOI":"10.3390\/molecules25204784"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"8391","DOI":"10.1039\/C8NJ00227D","article-title":"Improving the stability and reusability of dextranase by immobilization on polyethylenimine modified magnetic particles","volume":"42","author":"Wang","year":"2018","journal-title":"New J. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1016\/j.enzmictec.2007.01.018","article-title":"Improvement of enzyme activity, stability and selectivity via immobilization techniques","volume":"40","author":"Mateo","year":"2007","journal-title":"Enzym. Microb. Technol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"338","DOI":"10.12944\/CRNFSJ.5.3.19","article-title":"Production of exopolysaccharide from local fungal isolate","volume":"5","year":"2017","journal-title":"Curr. Res. Nutr. Food Sci. J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1007\/s00253-009-2323-y","article-title":"The inhibitory effects of mushroom extracts on sucrose-dependent oral biofilm formation","volume":"86","author":"Yano","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Pittrof, S.L., Kaufhold, L., Fischer, A., and Wefers, D. (2021). Products Released from Structurally Different Dextrans by Bacterial and Fungal Dextranases. Foods, 10.","DOI":"10.3390\/foods10020244"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1111\/febs.15074","article-title":"Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31","volume":"287","author":"Tsutsumi","year":"2020","journal-title":"FEBS J."},{"key":"ref_100","first-page":"33","article-title":"Advantages of Using the Dextranase Enzyme Based on Saccharomyces Cerevisiae in Beet Sugar Production","volume":"6","author":"Karpova","year":"2021","journal-title":"Int. Res. J."},{"key":"ref_101","unstructured":"Karpova, N.N., and Mogilevskaya, I.V. (2021, January 20). Selection of culture medium components for S. cerevisiae strain Y-1531-dextranase producer. Proceedings of the Annual Youth Scientific Conference, South of Russia: Challenges of Time, Discoveries, Prospects: Materials of the Conf, Rostov-on-Don, Russia."},{"key":"ref_102","unstructured":"Gres, N.A., and Skalny, A.V. (2011). Bioelemental Status of the Population of Belarus: Ecological, Physiological and Pathological Aspects, Harvest."},{"key":"ref_103","first-page":"59","article-title":"Kalbassa, Etiology, pathogenesis and treatment methods","volume":"3","author":"Volgin","year":"2006","journal-title":"Dent. Art."},{"key":"ref_104","first-page":"12","article-title":"Pikhur OL P Increased abrasion of hard dental tissues","volume":"2","author":"Tsimbalistov","year":"2005","journal-title":"Clin. Pict. Morphol. Cryst. Struct. Klin. Stomatol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.sjbs.2020.09.052","article-title":"Marine microorganisms as an untapped source of bioactive compounds","volume":"28","author":"Ameen","year":"2021","journal-title":"Saudi J. Biol. Sci."},{"key":"ref_106","first-page":"32","article-title":"Klinicheskie vozmojnosti primeneniya sovremennyih remineralizuyuschih sostavov u vzroslyih [Clinical possibilities of application of modern remineralizing compositions in adults]","volume":"3","author":"Fedorov","year":"2008","journal-title":"Clin. Stomatol."},{"key":"ref_107","first-page":"37","article-title":"Objective assessment method enamel mineral maturity and efficiency the effect of the drug \u201cCalcium-D3 Nycomed\u201d on the rate of maturation of hard tissues of permanent teeth in adolescents","volume":"3","author":"Kobiyasova","year":"2005","journal-title":"Dent. Forum"},{"key":"ref_108","first-page":"32","article-title":"Occlusal damage yak one of the primary reasons for vindication of non-carious cervical lesions","volume":"1","author":"Matviychuk","year":"2005","journal-title":"Bull. Dent."},{"key":"ref_109","first-page":"22","article-title":"Modern data on the mineral composition, structure and properties of hard dental tissues","volume":"2","author":"Ahmedbeyli","year":"2016","journal-title":"BioMed"},{"key":"ref_110","first-page":"116","article-title":"The role of dental plaque biofilm in oral health","volume":"81","author":"Gurenlian","year":"2007","journal-title":"Am. Dent. Hyg. Assoc."},{"key":"ref_111","first-page":"441","article-title":"Microbiology of dental plaque biofilms and their role in oral health and caries","volume":"54","author":"Marsh","year":"2010","journal-title":"Dent. Clin."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/j.tim.2005.09.006","article-title":"Oral microbial communities in sickness and in health","volume":"13","author":"Jenkinson","year":"2005","journal-title":"Trends Microbiol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1111\/j.1600-0528.2005.00232.x","article-title":"The complex oral microflora of high-risk individuals and groups and its role in the caries process","volume":"33","author":"Beighton","year":"2005","journal-title":"Commun. Dent. Oral Epidemiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1128\/MMBR.66.3.486-505.2002","article-title":"Communication among oral bacteria","volume":"66","author":"Kolenbrander","year":"2002","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1128\/CDLI.11.2.379-386.2004","article-title":"Establishment of an animal model using recombinant NOD. B10. D2 mice to study initial adhesion of oral streptococci","volume":"11","author":"Salam","year":"2004","journal-title":"Clin. Vaccine Immunol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1002\/yea.1311","article-title":"Cloning and characterization of a dextranase gene from Lipomyces starkeyi and its expression in Saccharomyces cerevisiae","volume":"22","author":"Kang","year":"2005","journal-title":"Yeast"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0003-9969(68)90042-3","article-title":"Enzymatic removal of artificial plaques","volume":"13","author":"Fitzgerald","year":"1968","journal-title":"Arch. Oral Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/0003-9969(69)90193-9","article-title":"Inhibition of insoluble dextran synthesis, plaque formation and dental caries in hamsters by low molecular weight dextran","volume":"14","author":"Gibbons","year":"1969","journal-title":"Arch. Oral Biol."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/17\/5533\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:19:09Z","timestamp":1760141949000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/17\/5533"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8,28]]},"references-count":118,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["molecules27175533"],"URL":"https:\/\/doi.org\/10.3390\/molecules27175533","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,8,28]]}}}