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Journal articles on the topic 'Dextranase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Pittrof, Silke L., Larissa Kaufhold, Anja Fischer, and Daniel Wefers. "Products Released from Structurally Different Dextrans by Bacterial and Fungal Dextranases." Foods 10, no. 2 (2021): 244. http://dx.doi.org/10.3390/foods10020244.

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Dextran hydrolysis by dextranases is applied in the sugar industry and the medical sector, but it also has a high potential for use in structural analysis of dextrans. However, dextranases are produced by several organisms and thus differ in their properties. The aim of this study was to comparatively investigate the product patterns obtained from the incubation of linear as well as O3- and O4-branched dextrans with different dextranases. For this purpose, genes encoding for dextranases from Bacteroides thetaiotaomicron and Streptococcus salivarius were cloned and heterologously expressed in E

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2

Huang, Ruijie, Lei Zhong, Fengwei Xie, et al. "Purification, Characterization and Degradation Performance of a Novel Dextranase from Penicillium cyclopium CICC-4022." International Journal of Molecular Sciences 20, no. 6 (2019): 1360. http://dx.doi.org/10.3390/ijms20061360.

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A novel dextranase was purified from Penicillium cyclopium CICC-4022 by ammonium sulfate fractional precipitation and gel filtration chromatography. The effects of temperature, pH and some metal ions and chemicals on dextranase activity were investigated. Subsequently, the dextranase was used to produce dextran with specific molecular mass. Weight-average molecular mass (Mw) and the ratio of weight-average molecular mass/number-average molecular mass, or polydispersity index (Mw/Mn), of dextran were measured by multiple-angle laser light scattering (MALS) combined with gel permeation chromatog

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3

Ding, Yanshuai, Hao Zhang, Xuelian Wang, et al. "Immobilization of Dextranase on Nano-Hydroxyapatite as a Recyclable Catalyst." Materials 14, no. 1 (2020): 130. http://dx.doi.org/10.3390/ma14010130.

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The immobilization technology provides a potential pathway for enzyme recycling. Here, we evaluated the potential of using dextranase immobilized onto hydroxyapatite nanoparticles as a promising inorganic material. The optimal immobilization temperature, reaction time, and pH were determined to be 25 °C, 120 min, and pH 5, respectively. Dextranase could be loaded at 359.7 U/g. The immobilized dextranase was characterized by field emission gun-scanning electron microscope (FEG-SEM), X-ray diffraction (XRD), and Fourier-transformed infrared spectroscopy (FT-IR). The hydrolysis capacity of the im

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4

Juntarachot, Nucharee, Sasithorn Sirilun, Duangporn Kantachote, et al. "Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste." PeerJ 8 (November 17, 2020): e10165. http://dx.doi.org/10.7717/peerj.10165.

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Background The accumulation of plaque causes oral diseases. Dental plaque is formed on teeth surfaces by oral bacterial pathogens, particularly Streptococcus mutans, in the oral cavity. Dextranase is one of the enzymes involved in antiplaque accumulation as it can prevent dental caries by the degradation of dextran, which is a component of plaque biofilm. This led to the idea of creating toothpaste containing dextranase for preventing oral diseases. However, the dextranase enzyme must be stable in the product; therefore, encapsulation is an attractive way to increase the stability of this enzy

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5

Baktir, Afaf, Zumrotul Koiriyah, and Ali Rohman. "A THERMOPHILIC MICROBE PRODUCING DEXTRANASE FROM HEATED SUGAR CANE." Indonesian Journal of Chemistry 5, no. 3 (2010): 224–27. http://dx.doi.org/10.22146/ijc.21794.

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A thermophilic aerobe microorganism designated NP4, was isolated from the heated sugar cane. It grew on dextran, and produced a thermoactive extracellular dextranase. Screening and isolation was done by assay of dextranase activity semi quantitatively on solid medium containing blue dextran. It provided several colonies with different morphology exhibited decolourized zones around, on culture plates containing blue dextran 2000R. The screening resulted in isolation of one microbe which efficiently assimilate dextran as carbon source. Dextranase production from the choised strain in liquid medi

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6

Juntarachot, Nucharee, Duangporn Kantachote, Sartjin Peerajan, Sasithorn Sirilun, and Chaiyavat Chaiyasut. "Optimization of Fungal Dextranase Production and Its Antibiofilm Activity, Encapsulation and Stability in Toothpaste." Molecules 25, no. 20 (2020): 4784. http://dx.doi.org/10.3390/molecules25204784.

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Dextranase catalyzes the degradation of the substrate dextran, which is a component of plaque biofilm. This enzyme is involved in antiplaque accumulation, which can prevent dental caries. The activity of crude dextranase from Penicillium roquefortii TISTR 3511 was assessed, and the maximum value (7.61 unit/g) was obtained at 37 °C and pH 6. The Plackett–Burman design was used to obtain significant factors for enhancing fungal dextranase production, and three influencing factors were found: Dextran, yeast extract concentration and inoculum age. Subsequently, the significant factors were optimiz

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7

Lai, Liu, Liu, et al. "The Marine Catenovulum agarivorans MNH15 and Dextranase: Removing Dental Plaque." Marine Drugs 17, no. 10 (2019): 592. http://dx.doi.org/10.3390/md17100592.

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Dextranase, a hydrolase that specifically hydrolyzes α-1,6-glucosidic bonds, has been used in the pharmaceutical, food, and biotechnology industries. In this study, the strain of Catenovulum agarivorans MNH15 was screened from marine samples. When the temperature, initial pH, NaCl concentration, and inducer concentration were 30 °C, 8.0, 5 g/L, and 8 g/L, respectively, it yielded more dextranase. The molecular weight of the dextranase was approximately 110 kDa. The maximum enzyme activity was achieved at 40 °C and a pH of 8.0. The enzyme was stable at 30 °C and a pH of 5–9. The metal ion Sr2+

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8

Shahid, Faiza, Afsheen Aman, and Shah Ali Ul Qader. "Immobilization of Dextranase Using Anionic Natural Polymer Alginate as a Matrix for the Degradation of a Long-Chain Biopolymer (Dextran)." International Journal of Polymer Science 2019 (March 31, 2019): 1–8. http://dx.doi.org/10.1155/2019/1354872.

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Alginate is an inexpensive, nontoxic, valuable biopolymer utilized in the study for the immobilization of commercially applicable biocatalyst dextranase. Dextranase was immobilized by an entrapment method, and alginate hydrogel spheres were synthesized after optimizing several parameters. A sodium alginate concentration of 4.0% was noticed to be suitable along with a calcium chloride concentration of 0.2 molar after providing a curing time of 20 minutes. After comparing the characteristics of the entrapped enzyme with those of the soluble one, it was observed that the characteristics were more

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9

Ebaya, Mahasen Mohamed Ahmed, Mohammed El-Mowafy, Mohamed Mohamed Adel El-Sokkary, and Ramadan Hassan. "Purification, Characterization, and Biocatalytic and Antibiofilm Activity of a Novel Dextranase from Talaromyces sp." International Journal of Microbiology 2020 (November 11, 2020): 1–11. http://dx.doi.org/10.1155/2020/9198048.

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Dextranase is a useful enzyme that catalyzes the degradation of dextran to low-molecular-weight fractions, which have many critical commercial and clinical applications. Endophytic fungi represent a source of both high heat-stable and pH-stable enzymes. In this study, from Delonix regia bark by plate assay, out of 12 isolated fungal strains, hyaline zones were detected in only one strain. By using the standard ITS rDNA sequencing analysis, the isolated strain was identified as Talaromyces sp. In the case of carbon source, in a medium containing 1% dextran T2000 as the sole carbon source, the m

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10

Esawy, Mona A., Sara H. Mansour, Eman F. Ahmed, Naziha M. Hassanein, and Hesham A. El Enshasy. "Characterization of Extracellular Dextranase from a Novel HalophilicBacillus subtilis NRC-B233ba Mutagenic Honey Isolate under Solid State Fermentation." E-Journal of Chemistry 9, no. 3 (2012): 1494–510. http://dx.doi.org/10.1155/2012/860619.

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Bacillus subtilis NRC-B233bwas isolated from Libyan honey sample proved to be a potent dextranase producer by applying solid state fermentation and utilizing corn flour as the sole carbon source. The optimized culture conditions for dextranase productions were 37°C, pH 10, 32 h, and 20% (v/w) moisture content. A unique character of this isolate is its ability to produce steady dextranase irrespective to the presence of NaCl in the medium. The addition of 0.175 Mm CrCl3 increased the enzyme production by about 4.5 fold. Further improvement in enzyme production was achieved by simple UV mutation

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11

Tongpong, Piyachat, Sasithorn Sirilun, Chaiyavat Chaiyasut, and Phakkharawat Sittiprapaporn. "The relationship between dextranase enzyme in mouthwash and dental caries." Asian Journal of Medical Sciences 11, no. 1 (2020): 80–84. http://dx.doi.org/10.3126/ajms.v11i1.26531.

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Background: Several studies reported that Thai people have oral health problems as a major problem. Therefore, care and treatment of oral health is an issue to be attentive. At the present, there are many products for oral and dental health care in many forms such as toothpaste, mouthwash, spray, deodorizing and inhibiting bacteria etc. Aims and Objective: This study investigated the effect of mouthwash containing Dextranase enzyme which affected to the changes of dental plaque (Plague Index) in eighteen dental caries volunteers by two mouthwash formulas; Formula I contained only Dextran

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12

Liu, Xin, Tian Deng, Xueqin Liu, et al. "Isomalto-Oligosaccharides Produced by Endodextranase Shewanella sp. GZ-7 From Sugarcane Plants." Natural Product Communications 15, no. 9 (2020): 1934578X2095328. http://dx.doi.org/10.1177/1934578x20953286.

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Oligosaccharides have important alimental and medical applications. Dextranase has been used to produce isomalto-oligosaccharides (IMOs). In this study, we isolated dextranase-producing bacteria from sugarcane-cultivated soil. Identification of the isolate based on its phenotypical, physiological, and biochemical characteristics, as well as 16S ribosomal deoxyribonucleic acid gene sequencing yielded Shewanella sp. strain GZ-7. The molecular weight of the dextranase produced by this strain was 100-135 kDa. The optimum temperature and pH for dextranase production were 40 °C and 7.5, respectively

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13

Larsson, Anna M., Rolf Andersson, Jerry Ståhlberg, Lennart Kenne, and T. Alwyn Jones. "Dextranase from Penicillium minioluteum." Structure 11, no. 9 (2003): 1111–21. http://dx.doi.org/10.1016/s0969-2126(03)00147-3.

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14

IGARASHI, Takeshi, and Nobuichi GOTO. "Dextranase of Streptococcus mutans." Nippon Saikingaku Zasshi 53, no. 2 (1998): 435–42. http://dx.doi.org/10.3412/jsb.53.435.

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15

HORITA, Munehiro, Terukazu KATSURO, Kunio OBAYASHI, and Hideshi AKAHORI. "Studies on dextranase production. Part I. Dextranase production in "fed-batch" culture." Journal of the agricultural chemical society of Japan 63, no. 4 (1989): 837–44. http://dx.doi.org/10.1271/nogeikagaku1924.63.837.

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16

Hijah, Vestika Iskawati Wahidul, Titi Candra Sunarti, and Anja Meryandini. "Production and Characteristics of Yeast Dextranase from Soil." HAYATI Journal of Biosciences 26, no. 1 (2019): 26. http://dx.doi.org/10.4308/hjb.26.1.26.

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The existence of dextran in sugar cane juice is a major problem in the sugar industry, causing substantial losses. Treatment of dextran through enzymatic hydrolysis using dextranase is highly recommended as the most suitable method at this time because this is more effective and more economical. This study investigated the production and characterization of dextranase from local isolate yeast to degrade dextran on sugar cane juice. The selected yeast was identified on the basis of molecular identification. Dextranase was produced from the culture with the best carbon and nitrogen sources then

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17

Liu, Hongfei, Wei Ren, Mingsheng Ly, Haifeng Li, and Shujun Wang. "Characterization of an Alkaline GH49 Dextranase from Marine Bacterium Arthrobacter oxydans KQ11 and Its Application in the Preparation of Isomalto-Oligosaccharide." Marine Drugs 17, no. 8 (2019): 479. http://dx.doi.org/10.3390/md17080479.

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A GH49 dextranase gene DexKQ was cloned from marine bacteria Arthrobacter oxydans KQ11. It was recombinantly expressed using an Escherichia coli system. Recombinant DexKQ dextranase of 66 kDa exhibited the highest catalytic activity at pH 9.0 and 55 °C. kcat/Km of recombinant DexKQ at the optimum condition reached 3.03 s−1 μM−1, which was six times that of commercial dextranase (0.5 s−1 μM−1). DexKQ possessed a Km value of 67.99 µM against dextran T70 substrate with 70 kDa molecular weight. Thin-layer chromatography (TLC) analysis showed that main hydrolysis end products were isomalto-oligosac

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18

Koenig, David W., and Donal F. Day. "Induction of Lipomyces starkeyi Dextranase." Applied and Environmental Microbiology 55, no. 8 (1989): 2079–81. http://dx.doi.org/10.1128/aem.55.8.2079-2081.1989.

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19

Rogalski, J., G. G?owiak, J. Szczodrak, M. Pleszczy?ska, Z. Szczodrak, and A. Wiater. "Purification and immobilization of dextranase." Acta Biotechnologica 18, no. 1 (1998): 63–75. http://dx.doi.org/10.1002/abio.370180111.

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20

Koenig, David W., and D. F. Day. "Production of dextranase byLipomyces starkeyi." Biotechnology Letters 10, no. 2 (1988): 117–22. http://dx.doi.org/10.1007/bf01024637.

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21

Leathers, Timothy D., Melinda S. Nunnally, and Gregory L. Côté. "Modification of alternan by dextranase." Biotechnology Letters 31, no. 2 (2008): 289–93. http://dx.doi.org/10.1007/s10529-008-9866-3.

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22

Madhu and K. A. Prabhu. "Immobilization of dextranase on bentonite." Enzyme and Microbial Technology 7, no. 6 (1985): 279–82. http://dx.doi.org/10.1016/0141-0229(85)90086-9.

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23

Liu, L., Y. Ding, S. Liu, S. Wang, Y. Fang, and M. Lyu. "Dextrans removal from sugarcane juice using dextranase from marine bacterium Arthrobacter oxydans KQ11." Quality Assurance and Safety of Crops & Foods 11, no. 1 (2019): 53–59. http://dx.doi.org/10.3920/qas2018.1289.

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24

Baktir, Afaf, and Kuntaman Kuntaman. "KEMAMPUAN TUMBUH Ecoli DH5 KOMPETEN DALAM 'MEDIUM MINIMAL' MENGANDUNG DEKSTRAN UNTUK MENGEMBANGKAN METODE SELEKSI KLON GEN DEKSTRANASE." Berkala Penelitian Hayati 7, no. 1 (2001): 53–59. http://dx.doi.org/10.23869/bphjbr.7.1.20017.

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Dextranase gene cloning so far have used selection method base on halo formation around he recombinant dex colony grown on LB blue dextran agar plate. The difficulty of the cloning process is in the selection of dex positive clone. As an example, for obtaining dex gene it has been screened about 36500 colonies. The reason that it was difficult to determine Dex positive clone because dextran hydrolysis by primary recombinant E. coli cells in LB blue dextran medium was too weak. In the present research, we have designed a minimal medium contained dextran and low concentration of yeast extract to

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25

Chu, Chong Woo, Je Ho Ryu, Young-IL Jeong, et al. "Redox-Responsive Nanophotosensitizer Composed of Chlorin e6-Conjugated Dextran for Photodynamic Treatment of Colon Cancer Cells." Journal of Nanomaterials 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/4075803.

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We synthesized dextran-chlorin e6 conjugates having disulfide linkage for specific targeting of colonic region and cancer cells. Reductive end group of dextran was treated with sodium borocyanohydride and conjugated with cystamine. Cystamine end group was conjugated with carboxylic acid of chlorin e6 (DEX6ss). DEX6ss conjugates were formed as spherical nanoparticles with small sizes less than 100 nm. Chlorin e6 (Ce6) was specifically released from DEX6ss nanoparticles in the presence of dextranase or glutathione (GSH), indicating that DEX6ss nanoparticles have responsiveness against dextranase

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26

Hanada, Nobuhiro, Tadamichi Takehara, Kohtaro Nakayama, and Eiichi Saeki. "Streptococcus mutans Serotype g Secrete Dextranase." Journal of the Kyushu Dental Society 40, no. 1 (1986): 323–28. http://dx.doi.org/10.2504/kds.40.323.

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27

KOENIG, DAVID W., and D. F. DAY. "Dextranase Production by a Derepressed Mutant." Annals of the New York Academy of Sciences 542, no. 1 Enzyme Engine (1988): 111–14. http://dx.doi.org/10.1111/j.1749-6632.1988.tb25814.x.

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28

Igarashi, Takeshi, Hirobumi Morisaki, and Nobuichi Goto. "Molecular Characterization of Dextranase fromStreptococcus rattus." Microbiology and Immunology 48, no. 3 (2004): 155–62. http://dx.doi.org/10.1111/j.1348-0421.2004.tb03501.x.

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29

Jiménez, Efraín Rodríguez. "Dextranase in sugar industry: A review." Sugar Tech 11, no. 2 (2009): 124–34. http://dx.doi.org/10.1007/s12355-009-0019-3.

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30

Finnegan, Patrick M., Stevens M. Brumbley, Michael G. O’Shea, Helena Nevalainen, and Peter L. Bergquist. "Diverse dextranase genes from Paenibacillus species." Archives of Microbiology 183, no. 2 (2005): 140–47. http://dx.doi.org/10.1007/s00203-004-0756-3.

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31

Erhardt, Frank Alwin, and Hans-Joachim Jördening. "Immobilization of dextranase from Chaetomium erraticum." Journal of Biotechnology 131, no. 4 (2007): 440–47. http://dx.doi.org/10.1016/j.jbiotec.2007.07.946.

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32

Burne, R. A., B. Rubinfeld, W. H. Bowen, and R. E. Yasbin. "Tight Genetic Linkage of a Glucosyltransferase and Dextranase of Streptococcus mutans GS-5." Journal of Dental Research 65, no. 12 (1986): 1392–401. http://dx.doi.org/10.1177/00220345860650120301.

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A genetic library consisting of over 5000 clones with an average insert size of 6.9 kilobasepairs (kbp) of Streptococcus mutans GS-5 has been constructed in a bivalent plasmid vector pMK3, which is capable of replicating in Escherichia coli and Bacillus subtilis. The recombinant plasmid pSUCRI, containing a 6.0 kbp fragment of S. mutans GS-5 DNA, was the focus of this study. Using Southern hybridization, in vitro and in vivo gene expression techniques, and biochemical analysis, this clone was shown to encode the 55 kiloDalton (kDal) GS-5 gtfA gene product, as well as a 38 and a 66 kDal polypep

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33

Wellington, Janet E., Janet M. Shaw, and Gwen J. Walker. "Dissociation and electrophoretic separation of dextranase and dextranase inhibitor from a tighly bound enzymeinhibitor complex ofStreptococcus sobrinus." Electrophoresis 14, no. 1 (1993): 613–18. http://dx.doi.org/10.1002/elps.1150140196.

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34

Wang, Yajie, Qiang Wang, Xiaoping Song, and Jingjing Cai. "Improving the stability and reusability of dextranase by immobilization on polyethylenimine modified magnetic particles." New Journal of Chemistry 42, no. 11 (2018): 8391–99. http://dx.doi.org/10.1039/c8nj00227d.

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35

Wynter, C. V. A., M. Chang, J. De Jersey, B. Patel, P. A. Inkerman, and S. Hamilton. "Isolation and characterization of a thermostable dextranase." Enzyme and Microbial Technology 20, no. 4 (1997): 242–47. http://dx.doi.org/10.1016/s0141-0229(96)00118-4.

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36

Igarashi, Takeshi, Ayako Yamamoto, and Nobuichi Goto. "Characterization of the Dextranase Purified fromStreptococcus mutansIngbritt." Microbiology and Immunology 36, no. 9 (1992): 969–76. http://dx.doi.org/10.1111/j.1348-0421.1992.tb02100.x.

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37

MIYAUCHI, Kouhei, Kunio SAWAMURA, Eiichi TAMIYA, and Isao KARUBE. "Determination of dextranase activity using enzyme sensor." NIPPON KAGAKU KAISHI, no. 3 (1987): 512–17. http://dx.doi.org/10.1246/nikkashi.1987.512.

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38

Lee, J. M., and P. F. Fox. "Purification and characterization of Paecilomyces lilacinus dextranase." Enzyme and Microbial Technology 7, no. 11 (1985): 573–77. http://dx.doi.org/10.1016/0141-0229(85)90103-6.

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39

Barrett, J. F., T. A. Barrett, and R. Curtiss. "Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sobrinus and cloning of the dextranase gene." Infection and Immunity 55, no. 3 (1987): 792–802. http://dx.doi.org/10.1128/iai.55.3.792-802.1987.

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40

Münkel, Franziska, and Daniel Wefers. "Fine structures of different dextrans assessed by isolation and characterization of endo-dextranase liberated isomalto-oligosaccharides." Carbohydrate Polymers 215 (July 2019): 296–306. http://dx.doi.org/10.1016/j.carbpol.2019.03.027.

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41

Wanda, S. Y., and R. Curtiss. "Purification and characterization of Streptococcus sobrinus dextranase produced in recombinant Escherichia coli and sequence analysis of the dextranase gene." Journal of Bacteriology 176, no. 13 (1994): 3839–50. http://dx.doi.org/10.1128/jb.176.13.3839-3850.1994.

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42

Takayanagi, Tsutomu. "Enzymological Studies on Isomalto-dextranase from Arthrobacter globiformis." Journal of Applied Glycoscience 49, no. 1 (2002): 57–62. http://dx.doi.org/10.5458/jag.49.57.

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43

Ölçer, Zehra, and Aziz Tanriseven. "Co-immobilization of dextransucrase and dextranase in alginate." Process Biochemistry 45, no. 10 (2010): 1645–51. http://dx.doi.org/10.1016/j.procbio.2010.06.011.

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44

Igarashi, T., A. Yamamoto, and N. Goto. "Detection of dextranase-producing gram-negative oral bacteria." Oral Microbiology and Immunology 13, no. 6 (1998): 382–86. http://dx.doi.org/10.1111/j.1399-302x.1998.tb00696.x.

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45

Igarashi, Takeshi, Ayako Yamamoto, and Nobuichi Goto. "Sequence Analysis of theStreptococcus mutansIngbrittdexAGene Encoding Extracellular Dextranase." Microbiology and Immunology 39, no. 11 (1995): 853–60. http://dx.doi.org/10.1111/j.1348-0421.1995.tb03282.x.

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46

Yamamoto, Kazuya, Kenji Yoshikawa, and Shigetaka Okada. "Substrate Specificity of Dextrin Dextranase fromAcetobacter capsulatusATCC 11894." Bioscience, Biotechnology, and Biochemistry 58, no. 2 (1994): 330–33. http://dx.doi.org/10.1271/bbb.58.330.

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47

Szczodrak, J., M. Pleszczyńska, and J. Fiedurek. "Penicillium notatum 1 a new source of dextranase." Journal of Industrial Microbiology 13, no. 5 (1994): 315–20. http://dx.doi.org/10.1007/bf01569734.

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48

El-Tanash, A. B., E. El-Baz, and A. A. Sherief. "Properties of Aspergillus subolivaceus free and immobilized dextranase." European Food Research and Technology 233, no. 5 (2011): 735–42. http://dx.doi.org/10.1007/s00217-011-1570-1.

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49

Bashari, Mohanad, Pei Wang, Ahmed Eibaid, Yaoqi Tian, Xueming Xu, and Zhengyu Jin. "Ultrasound-assisted dextranase entrapment onto Ca-alginate gel beads." Ultrasonics Sonochemistry 20, no. 4 (2013): 1008–16. http://dx.doi.org/10.1016/j.ultsonch.2012.11.016.

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50

Joncquiert, J. C., M. BÃ©chet, Y. Tierny, J. Courtois, H. C. Dubourguier, and J. B. Guillaume. "Cloning and expression inEscherichia coliof dextranase genes fromBacteroides thetaiotaomicron." FEMS Microbiology Letters 84, no. 3 (1991): 273–78. http://dx.doi.org/10.1111/j.1574-6968.1991.tb04609.x.

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