Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-galactooligosaccharides

Journal of Biotechnology - Tập 290 - Trang 44-52 - 2019
Panagiota Kalomoiri1, Jesper Holck1,2, Laure Coulomb3, Irene Boos1, Kasper Enemark-Rasmussen1, Nikolaj Spodsberg3, Rune Nygaard Monrad3, Mads H. Clausen1
1Center for Nanomedicine and Theranostics, Department of Chemistry, Technical University of Denmark, Kemitorvet 207, DK-2800, Kgs. Lyngby, Denmark
2Center for Bioprocess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
3Novozymes A/S, Krogshøjvej 36, DK-2880, Bagsværd, Denmark

Tài liệu tham khảo

Altschul, 1990, Basic local alignment search tool 2 department of computer science, J. Mol. Biol., 215, 403, 10.1016/S0022-2836(05)80360-2 Andersen, 2017, Synthesis and application of branched type II arabinogalactans, J. Org. Chem., 82, 12066, 10.1021/acs.joc.7b01796 Bairoch, 2000, The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000, Nucleic Acids Res., 28, 45, 10.1093/nar/28.1.45 Biely, 2014, Trichoderma reesei XYN VI – a novel appendage-dependent eukaryotic glucuronoxylan hydrolase, FEBS J., 281, 3894, 10.1111/febs.12925 Budolfsen, 2004 Cantarel, 2009, The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics, Nucleic Acids Res., 37, 233, 10.1093/nar/gkn663 Christensen, 1988, High-level expression of recombinant genes in Aspergillus oryzae, Bio/technology, 6, 1419 Deshpande, 2008, Protein glycosylation pathways in filamentous fungi, Glycobiology, 18, 626, 10.1093/glycob/cwn044 Ellis, 2010, Arabinogalactan-proteins: key regulators at the cell surface?, Plant. Physiol., 153, 403, 10.1104/pp.110.156000 Gao, 1999, Yariv reagent treatment induces programmed cell death in Arabidopsis cell cultures and implicates arabinogalactan protein involvement, Plant. J., 19, 321, 10.1046/j.1365-313X.1999.00544.x Hashimoto, 1971, Studies on the enzyme treatment of coffee beans part V. Structure of coffee arabinogalactan, Nippon Nogeikagaku Kaishi, 45, 147, 10.1271/nogeikagaku1924.45.147 Hashimoto, 1969, Studies on the enzyme treatment of coffee beans part III. Purification and some properties of galactanase from Rhizopus niveus, Nippon Nogeikagaku Kaishi, 43, 831, 10.1271/nogeikagaku1924.43.831 Henrissat, 1997, Structural and sequence-based classification of glycoside hydrolases, Curr. Opin. Struct. Biol., 7, 637, 10.1016/S0959-440X(97)80072-3 Kotake, 2011, Endo-β-1,3-galactanase from winter mushroom Flammulina velutipes, J. Biol. Chem., 286, 27848, 10.1074/jbc.M111.251736 Lever, 1977, Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): effect of bismuth on the reaction, Anal. Biochem., 81, 21, 10.1016/0003-2697(77)90594-2 Ling, 2012, An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure, Carbohydr. Res., 352, 70, 10.1016/j.carres.2012.02.033 Mahendran, 2008, New insights into the structural characteristics of the arabinogalactan – protein (AGP) fraction of gum Arabic, J. Agric. Food Chem., 56, 9269, 10.1021/jf800849a McBrayer, B., Shaghasi, T., Vlasenko, E., 2011. Compositions for saccharification of cellulosic material International patent application WO/2011/057140. Nie, 2013, A further amendment to the classical core structure of gum arabic (Acacia senegal), Food Hydrocoll., 31, 42, 10.1016/j.foodhyd.2012.09.014 Pereira, 2015, Arabinogalactan proteins: rising attention from plant biologists, Plant. Reprod., 28, 1, 10.1007/s00497-015-0254-6 Sakamoto, 2013, Peculiarities and applications of galactanolytic enzymes that act on type i and II arabinogalactans, Appl. Microbiol. Biotechnol., 97, 5201, 10.1007/s00253-013-4946-2 Schnorr, K.M., Anderson, L., Da Fonseca, M.L.Q.C., Leite, R., 2015. Expression constructs comprising a Terebella lapidaria nucleic acid encoding a cellulase, host cells, and methods of making the cellulase United States Patent US9000138B2. Serpe, 1994, Effects of yariv phenylglycosides on rosa cell-suspensions: evidence for the involvement of arabinogalactan-proteins in cell-proliferation, Planta, 193, 542, 10.1007/BF02411560 Showalter, 2001, Arabinogalactan-proteins: structure, expression and function, Cell. Mol. Life Sci., 58, 1399, 10.1007/PL00000784 Tsumuraya, 1984, Structure of L-arabino-D-galactan-containing proteins from radish leaves, Carbohydr. Res., 134, 215, 10.1016/0008-6215(84)85039-9 Tsumuraya, 1990, Purification of an exo-beta-(-3)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins, J. Biol. Chem., 265, 7207, 10.1016/S0021-9258(19)39100-8 Van Hengel, 2002, Fucosylated arabinogalactan-proteins are required for full root cell elongation in Arabidopsis, Plant. J., 32, 105, 10.1046/j.1365-313X.2002.01406.x Yoshimi, 2017, Properties of two fungal endo-β-1,3-galactanases and their synergistic action with an exo-β-1,3-galactanase in degrading arabinogalactan-proteins, Carbohydr. Res., 453–454, 26, 10.1016/j.carres.2017.10.013