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University of Groningen Identification and characterization of glycoside hydrolase family 32 enzymes from Aspergillus niger Goosen, Coenie IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2007 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Goosen, C. (2007). Identification and characterization of glycoside hydrolase family 32 enzymes from Aspergillus niger. s.n. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 02-10-2021 References REFERENCES Abarca, M. L., Accensi, F., Cano, J. & Cabanes, F. J. (2004). Taxonomy and significance of black aspergilli. Antonie Van Leeuwenhoek 86 , 33-49. Akimoto, H., Kushima, T., Nakamura, T. & Ohta, K. (1999). Transcriptional analysis of two endoinulinase genes inuA and inuB in Aspergillus niger and nucleotide sequences of their promoter regions. J Biosci Bioeng 88 , 599–604. Akimoto, H., Kiyota, N., Kushima, T., Nakamura, T. & Ohta, K. (2000). Molecular cloning and sequence analysis of an endoinulinase gene from Penicillium sp. strain TN-88. Biosci Biotechnol Biochem 64 , 2328-2335. Alberto, F., Bignon, C., Sulzenbacher, G., Henrissat, B. & Czjzek, M. (2004). The three- dimensional structure of invertase ( β-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J Biol Chem 279 , 18903-18910. Alberto, F., Jordi, E., Henrissat, B. & Czjzek, M. (2006). Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochem J 395 , 457-462. Altenbach, D., Nuesch, E., Ritsema, T., Boller, T. & Wiemken, A. (2005). Mutational analysis of the active center of plant fructosyltransferases: Festuca 1-SST and barley 6-SFT. FEBS Lett 579 , 4647-4653. Arand, M., Golubev, A. M., Neto, J. R. N. & other authors (2002). Purification, charaterization, gene cloning and preliminary X-ray data of the exo-inulase from Aspergillus awamori . Biochem J 362 , 131-135. 141 References Arnold, J. & Hilton, N. (2003). Genome sequencing: Revelations from a bread mould. Nature 422 , 821-822. Bach Knudsen, K. E. & Hessov, I. (1995). Recovery of inulin from Jerusalem artichoke (Helianthus tuberosus L .) in the small intestine of man. Br J Nutr 74 , 101-113. Bairoch, A. (2000). The ENZYME database in 2000. Nucleic Acids Res 28 , 304-305. Balakrishnan, M., Simmonds, R. S. & Tagg, J. R. (2006). Dental caries is a preventable infectious disease. Aust Dent J 45 , 235-245. Barbier, O., Girard, C., Breton, R., Belanger, A. & Hum, D. W. (2000). N-glycosylation and residue 96 are involved in the functional properties of UDP-glucuronosyltransferase enzymes. Biochemistry 39 , 11540-11552. Batista, F. R., Hernandez, L., Fernandez, J. R., Arrieta, J., Menendez, C., Gomez, R., Tambara, Y. & Pons, T. (1999). Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity. Biochem J 337 , 503-506. Beisel, H. G., Kawabata, S., Iwanaga, S., Huber, R. & Bode, W. (1999). Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus . Embo J 18 , 2313-2322. Bendtsen, J. D., Jensen, L. J., Blom, N., von Heijne, G. & Brunak, S. (2004). Feature- based prediction of non-classical and leaderless protein secretion. Protein Eng Des Sel 17 , 349–356. Bennet, J. W., Lasure, L. L., Bennet, J. W. & Lasure, L. L. (1991). Growth Media. In More gene manipulation in fungi , pp. 441-457. New York: Academic Press. Bhatti, H. N., Asgher, M., Abbas, A., Nawaz, R. & Sheikh, M. A. (2006). Studies on kinetics and thermostability of a novel acid invertase from Fusarium solani J Agric Food Chem 54 , 4617-4623. 142 References Boddy, L. M., Berges, T., Barreau, C., Vainstein, M. H., Dobson, M. J., Ballance, D. J. & Peberdy, J. F. (1993). Purification and characterisation of an Aspergillus niger invertase and its DNA sequence. Curr Genet 24 , 60-66. Bos, C. J., Debets, A. J., Swart, K., Huybers, A., Kobus, G. & Slakhorst, S. M. (1988). Genetic analysis and the construction of master strains for assignment of genes to six linkage groups in Aspergillus niger. Curr Genet 14 , 437-443. Burne, R. A. & Penders, J. E. (1992). Characterization of the Streptococcus mutans GS-5 fruA gene encoding exo-beta-D-fructosidase. Infect Immun 60 , 4621-4632. Cairns, A. J. & Ashton, J. E. (1991). The interpretation of in vitro measurements of fructosyl transferase activity: an analysis of patterns of fructosyl transfer by fungal invertase. New Phytol 118 , 24-33. Cairns, A. J. (2003). Fructan biosynthesis in transgenic plants. J Exp Bot 54 , 549-567. Carroll, S. B. (2003). Genetics and the making of Homo sapiens . Nature 422 , 849-857. Cerning, J. (1990). Exocellular polysaccharides produced by lactic acid bacteria. FEMS Microbiol Rev 87 , 113-130. Cha´vez, F. P., Pons, T., Delgado, J. M. & Rodrı´guez, L. (1998). Cloning and sequence analysis of the gene encoding invertase (INV1) from the yeast Candida utilis. Yeast 14 , 1223– 1232. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G. & Thompson, J. D. (2003) . Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res 31 , 3497–3500 Chiou, C. Y., Wang, H. H. & Shaw, G. C. (2002). Identification and characterization of the non-PTS fru locus of Bacillus megaterium ATCC 14581. Mol Genet Genomics 268 , 240–248. 143 References Collins, F. S., Green, E. D., Guttmacher, A. E. & Guyer, M. S. (2003a). A vision for the future of genomics research. Nature 422 , 835-847. Collins, F. S., Morgan, M. & Patrinos, A. (2003b). The Human Genome Project: lessons from large-scale biology. Science 300 , 286-290. Coudray, C., Rambeau, M., Feillet-Coudray, C., Tressol, J. C., Demigne, C., Gueux, E., Mazur, A. & Rayssiguier, Y. (2005). Dietary inulin intake and age can significantly affect intestinal absorption of calcium and magnesium in rats: a stable isotope approach. Nutr J 4, 29. Coutinho, P. M., Henrissat, B., Gilbert, H. J., Davies, G., Henrissat, B. & Svensson, B. (1999). Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering , pp. 3-12. Cambridge: The Royal Society of Chemistry. Crooks, G. E., Hon, G., Chandonia, J. M. & Brenner, S. E. (2004). WebLogo: a sequence logo generator. Genome Res 14 , 1188-1190. Cummings, J. H., Macfarlane, G. T. & Englyst, H. N. (2001). Prebiotic digestion and fermentation. Am J Clin Nutr 73 , 415S-420S. Davies, G. & Henrissat, B. (1995). Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859. Davies, G. J., Wilson, K. S. & Henrissat, B. (1997). Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321 , 557-559. Delzenne, N. M. & Kok, N. (2001). Effects of fructan-type prebiotics on lipid metabolism. Am J Clin Nutr 73 , 456-458. de Ruiter-Jacobs, Y. M., Broekhuijsen, M., Unkles, S. E., Campbell, E. I., Kinghorn, J. R., Contreras, R., Pouwels, P. H. & van den Hondel, C. A. (1989). A gene transfer system based on the homologous pyrG gene and efficient expression of bacterial genes in Aspergillus oryzae. Curr Genet 16 , 159-163. 144 References de Vries, R. P., van Grieken, C., van Kuyk, P. A. & Wo¨ sten, H. A. B. (2005). The value of genome sequences in the rapid identification of novel genes encoding specific plant cell wall degrading enzymes. Curr Genom 6, 157–187. Dorta, C., Cruz, R., de Oliva-Neto, P. & Moura, D. J. (2006). Sugarcane molasses and yeast powder used in the Fructooligosaccharides production by Aspergillus japonicus -FCL 119T and Aspergillus niger ATCC 20611. J Ind Microbiol Biotechnol 33 , 1003-1009. Dowzer, C. E. & Kelly, J. M. (1991). Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans . Mol Cell Biol 11 , 5701-5709. Druart, N., De Roover, J., Van den Ende, W., Goupil, P., Van Laere, A. & Rambour, S. (2001). Sucrose assimilation during early developmental stages of chicory ( Cichorium intybus L.) plants. Planta 212 , 436-443. Eddy, S. R. (1998). Profile hidden Markov models. Bioinformatics 14 , 755–763. Ettalibi, M. & Baratti, J. C. (1987). Purification, properties and comparison of invertase, exoinulinases and endoinulinases of Aspergillus ficuum. Appl Microbiol Biotechnol 26 , 13-20. Ettalibi, M. & Baratti, J. C. (2001). Sucrose hydrolysis by thermostable immobilized inulinases from Aspergillus ficuum . Enzyme Microb Technol 28 , 596-601. Fleischmann, R. D., Adams, M. D., White, O. & other authors (1995). Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269 , 496-512. Frazier, M. E., Johnson, G. M., Thomassen, D. G., Oliver, C. E. & Patrinos, A. (2003). Realizing the potential of the genome revolution: The Genomes to Life Program. Science 300 , 290-293. Fuchs, A., de Bruijn, J. M. & Niedeveld, C. J. (1983). Bacteria and yeasts as possible candidates for the production of inulinases and levanases.
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  • Sig Ski Ward, Jennifer F. Bryan

    Sig Ski Ward, Jennifer F. Bryan

    US009181319B2 (12) United States Patent (10) Patent No.: US 9,181,319 B2 Schrum et al. (45) Date of Patent: Nov. 10, 2015 (54) ENGINEERED NUCLEICACIDS AND 4,401,796 A 8, 1983 Itakura METHODS OF USE THEREOF 4411,657 A 10, 1983 Galindo 4.415,732 A 11/1983 Caruthers et al. 4,458,066 A 7/1984 Caruthers et al. (71) Applicant: Moderna Therapeutics, Inc., 4.474,569 A 10, 1984 Newkirk Cambridge, MA (US) 4,500,707 A 2/1985 Caruthers et al. 4,579,849 A 4, 1986 MacCoSS et al. (72) Inventors: Jason P. Schrum, Philadelphia, PA 4,588,585 A 5/1986 Market al. (US); Stephane Bancel, Cambridge, MA is, A 38. Athlet al. (US); Noubar B. Afeyan, Cambridge, 4,816,567- A 3/1989 Cabillyak ( eta. al. MA (US) 4,879,111 A 1 1/1989 Chong 4,957,735 A 9/1990 Huang (73) Assignee: Moderna Therapeutics, Inc., 4.959,314 A 9, 1990 Market al. Cambridge, MA (US) 4,973,679 A 11/1990 Caruthers et al. s 5,012,818 A 5/1991 Joishy (*) Notice: Subject to any disclaimer, the term of this 3. A &E El al. patent is extended or adjusted under 35 5,036,006 A 7, 1991 Sanford et al. U.S.C. 154(b) by 0 days. 5,047,524. A 9/1991 Andrus et al. 5,116,943 A 5/1992 Koths et al. (21) Appl. No.: 14/270,736 5,130,238 A 7, 1992 Malek et al. 5,132,418 A 7, 1992 Caruthers et al.
  • Functional Characterization of Sucrose Phosphorylase and Scrr, a Regulator Of

    Functional Characterization of Sucrose Phosphorylase and Scrr, a Regulator Of

    1 Functional characterization of sucrose phosphorylase and scrR, a regulator of 2 sucrose metabolism in Lactobacillus reuteri 3 4 Januana S. Teixeira1, Reihaneh Abdi1,2, Marcia Shu-Wei Su1,3, Clarissa Schwab1,4, and 5 Michael G. Gänzle 1§ 6 7 1University of Alberta, Department of Agricultural, Food and Nutritional Science, 8 Edmonton, Canada 9 2Isfahan University of Technology, Department of Food Science, College of Agriculture, 10 Isfahan, Iran 11 3Present address, Pennsylvania State University, Department of Biology, University Park, 12 PA, U.S.A. 13 4Present address, University of Vienna, Department of Genetics in Ecology, Vienna, 14 Austria 15 16 §Corresponding author 17 4- 10 Ag/For Centre 18 Edmonton, AB, T6G 2P5 19 Canada 20 21 e-mail, [email protected] 22 phone, + 1 780 492 0774 23 fax, + 1 780 492 4265 24 1 25 Abstract 26 Lactobacillus reuteri harbors alternative enzymes for sucrose metabolism, sucrose 27 phosphorylase, fructansucrases, and glucansucrases. Sucrose phosphorylase and 28 fructansucrases additionally contribute to raffinose metabolism. Glucansucrases and 29 fructansucrases produce exopolysaccharides as alternative to sucrose hydrolysis. L. 30 reuteri LTH5448 expresses a levansucrase (ftfA) and sucrose phosphorylase (scrP), both 31 are inducible by sucrose. This study determined the contribution of scrP to sucrose and 32 raffinose metabolism in L. reuteri LTH5448, and elucidated the role of scrR in regulation 33 sucrose metabolism. Disruption of scrP and scrR was achieved by double crossover 34 mutagenesis. L. reuteri LTH5448, LTH5448ΔscrP and LTH5448ΔscrR were 35 characterized with respect to growth and metabolite formation with glucose, sucrose, or 36 raffinose as sole carbon source. Inactivation of scrR led to constitutive transcription of 37 scrP and ftfA, demonstrating that scrR is negative regulator.
  • Cloning and Expression of Levansucrase Gene of Bacillus Velezensis BM-2 and Enzymatic Synthesis of Levan

    Cloning and Expression of Levansucrase Gene of Bacillus Velezensis BM-2 and Enzymatic Synthesis of Levan

    processes Article Cloning and Expression of Levansucrase Gene of Bacillus velezensis BM-2 and Enzymatic Synthesis of Levan Min Xu, Lixia Zhang, Fangkun Zhao, Jingyue Wang, Bo Zhao, Zhijiang Zhou * and Ye Han School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China; [email protected] (M.X.); [email protected] (L.Z.); [email protected] (F.Z.); [email protected] (J.W.); [email protected] (B.Z.); [email protected] (Y.H.) * Correspondence: [email protected]; Tel.: +86-022-13920209057 Abstract: Levan is a versatile and valuable fructose homopolymer, and a few bacterial strains have been found to produce levan. Although levan products have numerous specific functions, their application and promotion were limited by the production capacity and production cost. Bacillus velezensis BM-2 is a levan-synthesizing strain, but its levan production is too low to apply. In this study, the levansucrase gene of B. velezensis BM-2 was cloned to plasmid pET-32a-Acma-zz, and the recombinant plasmids were transferred to Escherichia coli BL21. A transformed clone was selected to express and secrete the fusion enzymes with an Acma-tag efficiently. The expressed products were further purified by a self-developed separating material called bacterial enhancer matrix (BEM) particles. The purification efficiency was 93.4%, with a specific activity of 16.589 U/mL protein. The enzymatic reaction results indicated that the optimal reaction temperature is 50 ◦C, the optimal pH of the acetate buffer is 5.6, and the buffer system greatly influenced the enzyme activity. The enzyme activity was enhanced to 130% in the presence of 5 mM Ca2+,K+, Zn2+, and Mn2+, whereas it was 2+ 3+ almost abolished in the case of Cu and Fe .