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Volumn 3, Issue SEP, 2015, Pages

Underpinning starch biology with in vitro studies on carbohydrate-active enzymes and biosynthetic glycomaterials

Author keywords

Glucans; Nanotechnology; Phosphorylase; Self assembly; Starch; Synthetic biology

Indexed keywords

BIOSYNTHESIS; CRYSTALLINE MATERIALS; ENZYMES; METAL NANOPARTICLES; NANOTECHNOLOGY; PHASE INTERFACES; PLANTS (BOTANY); SELF ASSEMBLY;

EID: 85020977359     PISSN: None     EISSN: 22964185     Source Type: Journal    
DOI: 10.3389/fbioe.2015.00136     Document Type: Short Survey
Times cited : (20)

References (61)
  • 1
    • 0142040430 scopus 로고    scopus 로고
    • From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule
    • Ball, S. G., and Morell, M. K. (2003). From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu. Rev. Plant Biol. 54, 207-233. doi: 10.1146/annurev.arplant.54.031902.134927
    • (2003) Annu. Rev. Plant Biol , vol.54 , pp. 207-233
    • Ball, S.G.1    Morell, M.K.2
  • 2
    • 1542277660 scopus 로고    scopus 로고
    • Starch paste stickiness is a relevant native starch selection criterion for wet-end paper manufacturing
    • Blennow, A., Bay-Smidt, A. M., Leonhardt, P., Bandsholm, O., and Madsen, M. H. (2003). Starch paste stickiness is a relevant native starch selection criterion for wet-end paper manufacturing. Starch. Stärke 55, 381-389. doi:10.1002/star.200300169
    • (2003) Starch. Stärke , vol.55 , pp. 381-389
    • Blennow, A.1    Bay-Smidt, A.M.2    Leonhardt, P.3    Bandsholm, O.4    Madsen, M.H.5
  • 3
    • 35148833781 scopus 로고    scopus 로고
    • Self-association and crystallization of amylose
    • Buleon, A., Veronese, G., and Putaux, J. L. (2007). Self-association and crystallization of amylose. Aust. J. Chem. 60, 706-718. doi:10.1071/ch07168
    • (2007) Aust. J. Chem , vol.60 , pp. 706-718
    • Buleon, A.1    Veronese, G.2    Putaux, J.L.3
  • 4
    • 1242274329 scopus 로고    scopus 로고
    • Starch granule initiation is controlled by a heteromultimeric isoamylase in potato tubers
    • Bustos, R., Fahy, B., Hylton, C. M., Seale, R., Nebane, N. M., Edwards, A., et al. (2004). Starch granule initiation is controlled by a heteromultimeric isoamylase in potato tubers. Proc. Natl. Acad. Sci. U.S.A. 101, 2215-2220. doi:10.1073/pnas.0305920101
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 2215-2220
    • Bustos, R.1    Fahy, B.2    Hylton, C.M.3    Seale, R.4    Nebane, N.M.5    Edwards, A.6
  • 5
    • 56449128052 scopus 로고    scopus 로고
    • Detection of transglucosidase-catalyzed polysaccharide synthesis on a surface in real time using surface plasmon resonance spectroscopy
    • Cle, C., Gunning, A. P., Syson, K., Bowater, L., Field, R. A., and Bornemann, S. (2008). Detection of transglucosidase-catalyzed polysaccharide synthesis on a surface in real time using surface plasmon resonance spectroscopy. J. Am. Chem. Soc. 130, 15234-15235. doi:10.1021/ja805264w
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 15234-15235
    • Cle, C.1    Gunning, A.P.2    Syson, K.3    Bowater, L.4    Field, R.A.5    Bornemann, S.6
  • 6
    • 71549142345 scopus 로고    scopus 로고
    • Detection of enzyme-catalyzed polysaccharide synthesis on surfaces
    • Cle, C., Martin, C., Field, R. A., Kuzmic, P., and Bornemann, S. (2010). Detection of enzyme-catalyzed polysaccharide synthesis on surfaces. Biocatal. Biotransformation 28, 64-71. doi:10.3109/10242420903388744
    • (2010) Biocatal. Biotransformation , vol.28 , pp. 64-71
    • Cle, C.1    Martin, C.2    Field, R.A.3    Kuzmic, P.4    Bornemann, S.5
  • 8
    • 78650758060 scopus 로고    scopus 로고
    • Engineering the chloroplast targeted malarial vaccine antigens in Chlamydomonas starch granules
    • Dauvillée, D., Delhaye, S., Gruyer, S., Slomianny, C., Moretz, S. E., d'Hulst, C., et al. (2010). Engineering the chloroplast targeted malarial vaccine antigens in Chlamydomonas starch granules. PLoS ONE 5:e15424. doi:10.1371/journal.pone.0015424
    • (2010) PLoS ONE , vol.5
    • Dauvillée, D.1    Delhaye, S.2    Gruyer, S.3    Slomianny, C.4    Moretz, S.E.5    d'Hulst, C.6
  • 9
    • 71849119813 scopus 로고    scopus 로고
    • FAO's director-general on how to feed the world in 2050
    • Diouf, J. (2009). FAO's director-general on how to feed the world in 2050. Popul. Dev. Rev. 35, 837-839. doi:10.1111/j.1728-4457.2009.00312.x
    • (2009) Popul. Dev. Rev , vol.35 , pp. 837-839
    • Diouf, J.1
  • 10
    • 34548679587 scopus 로고    scopus 로고
    • Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases
    • Edner, C., Li, J., Albrecht, T., Mahlow, S., Hejazi, M., Hussain, H., et al. (2007). Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases. Plant Physiol. 145, 17-28. doi:10.1104/pp.107.104224
    • (2007) Plant Physiol , vol.145 , pp. 17-28
    • Edner, C.1    Li, J.2    Albrecht, T.3    Mahlow, S.4    Hejazi, M.5    Hussain, H.6
  • 13
    • 0031008546 scopus 로고    scopus 로고
    • Further syntheses employing phosphorylase
    • Evers, B., and Thiem, J. (1997). Further syntheses employing phosphorylase. Bioorg. Med. Chem. 5, 857-863. doi:10.1016/S0968-0896(97)00031-X
    • (1997) Bioorg. Med. Chem , vol.5 , pp. 857-863
    • Evers, B.1    Thiem, J.2
  • 14
    • 66649116284 scopus 로고    scopus 로고
    • Eukaryotic starch degradation: integration of plastidial and cytosolic pathways
    • Fettke, J., Hejazi, M., Smirnova, J., Hochel, E., Stage, M., and Steup, M. (2009). Eukaryotic starch degradation: integration of plastidial and cytosolic pathways. J. Exp. Bot. 60, 2907-2922. doi:10.1093/jxb/erp054
    • (2009) J. Exp. Bot , vol.60 , pp. 2907-2922
    • Fettke, J.1    Hejazi, M.2    Smirnova, J.3    Hochel, E.4    Stage, M.5    Steup, M.6
  • 15
    • 0020486663 scopus 로고
    • Potato and rabbit muscle phosphorylases-comparative studies on the structure, function and regulation of regulatory and non-regulatory enzymes
    • Fukui, T., Shimomura, S., and Nakano, K. (1982). Potato and rabbit muscle phosphorylases-comparative studies on the structure, function and regulation of regulatory and non-regulatory enzymes. Mol. Cell. Biochem. 42, 129-144. doi:10.1007/BF00238507
    • (1982) Mol. Cell. Biochem , vol.42 , pp. 129-144
    • Fukui, T.1    Shimomura, S.2    Nakano, K.3
  • 16
    • 25844469518 scopus 로고    scopus 로고
    • Potato phosphorylase catalyzed synthesis of amylose-lipid complexes
    • Gelders, G. G., Goesaert, H., and Delcour, J. A. (2005). Potato phosphorylase catalyzed synthesis of amylose-lipid complexes. Biomacromolecules 6, 2622-2629. doi:10.1021/bm0502011
    • (2005) Biomacromolecules , vol.6 , pp. 2622-2629
    • Gelders, G.G.1    Goesaert, H.2    Delcour, J.A.3
  • 17
    • 84880104830 scopus 로고    scopus 로고
    • Enzymatic reactions on immobilised substrates
    • Gray, C. J., Weissenborn, M. J., Eyers, C. E., and Flitsch, S. L. (2013). Enzymatic reactions on immobilised substrates. Chem. Soc. Rev. 42, 6378-6405. doi:10.1039/C3CS60018A
    • (2013) Chem. Soc. Rev , vol.42 , pp. 6378-6405
    • Gray, C.J.1    Weissenborn, M.J.2    Eyers, C.E.3    Flitsch, S.L.4
  • 19
    • 0015503871 scopus 로고
    • Characterization of Pseudomonas isoamylase by its actions on amylopectin and glycogen: comparison with Aerobacter pullulanase
    • Harada, T., Misaki, A., Akai, H., Yokobayashi, K., and Sugimoto, K. (1972). Characterization of Pseudomonas isoamylase by its actions on amylopectin and glycogen: comparison with Aerobacter pullulanase. Biochim Biophys Acta 268, 497-505. doi:10.1016/0005-2744(72)90345-2
    • (1972) Biochim Biophys Acta , vol.268 , pp. 497-505
    • Harada, T.1    Misaki, A.2    Akai, H.3    Yokobayashi, K.4    Sugimoto, K.5
  • 20
    • 66649091188 scopus 로고    scopus 로고
    • The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the A-and B-type allomorphs of crystallized maltodextrins but the mode of action differs
    • Hejazi, M., Fettke, J., Paris, O., and Steup, M. (2009). The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the A-and B-type allomorphs of crystallized maltodextrins but the mode of action differs. Plant Physiol. 150, 962-976. doi:10.1104/pp.109.138750
    • (2009) Plant Physiol , vol.150 , pp. 962-976
    • Hejazi, M.1    Fettke, J.2    Paris, O.3    Steup, M.4
  • 21
    • 1542380999 scopus 로고    scopus 로고
    • Improving starch for food and industrial applications
    • Jobling, S. (2004). Improving starch for food and industrial applications. Curr. Opin. Plant Biol. 7, 210-218. doi:10.1016/j.pbi.2003.12.001
    • (2004) Curr. Opin. Plant Biol , vol.7 , pp. 210-218
    • Jobling, S.1
  • 22
    • 0036195311 scopus 로고    scopus 로고
    • Production of a freeze-thaw-stable potato starch by antisense inhibition of three starch synthase genes
    • Jobling, S. A., Westcott, R. J., Tayal, A., Jeffcoat, R., and Schwall, G. P. (2002). Production of a freeze-thaw-stable potato starch by antisense inhibition of three starch synthase genes. Nat. Biotechnol. 20, 295-299. doi:10.1038/nbt0302-295
    • (2002) Nat. Biotechnol , vol.20 , pp. 295-299
    • Jobling, S.A.1    Westcott, R.J.2    Tayal, A.3    Jeffcoat, R.4    Schwall, G.P.5
  • 23
    • 84925796367 scopus 로고    scopus 로고
    • Synthesis of chitin and chitosan stereoisomers by thermostable a-glucan phosphorylase-catalyzed enzymatic polymerization of a-D-glucosamine 1-phosphate
    • Kadokawa, J., Shimohigoshi, R., Yamashita, K., and Yamamoto, K. (2015). Synthesis of chitin and chitosan stereoisomers by thermostable a-glucan phosphorylase-catalyzed enzymatic polymerization of a-D-glucosamine 1-phosphate. Org. Biomol. Chem. 13, 4336-4343. doi:10.1039/C5OB00167F
    • (2015) Org. Biomol. Chem , vol.13 , pp. 4336-4343
    • Kadokawa, J.1    Shimohigoshi, R.2    Yamashita, K.3    Yamamoto, K.4
  • 24
    • 38049062085 scopus 로고    scopus 로고
    • Chemoenzymatic syntheses of amylose-grafted chitin and chitosan
    • Kaneko, Y., Matsuda, S., and Kadokawa, J. (2007). Chemoenzymatic syntheses of amylose-grafted chitin and chitosan. Biomacromolecules 8, 3959-3964. doi:10.1021/bm701000t
    • (2007) Biomacromolecules , vol.8 , pp. 3959-3964
    • Kaneko, Y.1    Matsuda, S.2    Kadokawa, J.3
  • 26
    • 39049133868 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays
    • Karamanska, R., Clarke, J., Blixt, O., MacRae, J., Zhang, J., Crocker, P., et al. (2008). Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays. Glycoconj. J. 25, 69-74. doi:10.1007/s10719-007-9047-y
    • (2008) Glycoconj. J , vol.25 , pp. 69-74
    • Karamanska, R.1    Clarke, J.2    Blixt, O.3    MacRae, J.4    Zhang, J.5    Crocker, P.6
  • 27
    • 77649155700 scopus 로고    scopus 로고
    • Phosphorylase-catalyzed N-formyl-a-glucosaminylation of maltooligosaccharides
    • Kawazoe, S., Izawa, H., Nawaji, M., Kaneko, Y., and Kadokawa, J. (2010). Phosphorylase-catalyzed N-formyl-a-glucosaminylation of maltooligosaccharides. Carbohydr. Res. 345, 631-636. doi:10.1016/j.carres.2010.01.001
    • (2010) Carbohydr. Res , vol.345 , pp. 631-636
    • Kawazoe, S.1    Izawa, H.2    Nawaji, M.3    Kaneko, Y.4    Kadokawa, J.5
  • 28
    • 0020488546 scopus 로고
    • General acid-base catalysis of a-glucan phosphorylases-stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and ortho-phosphate (arsenate) dependent reaction
    • Klein, H. W., Palm, D., and Helmreich, E. J. M. (1982). General acid-base catalysis of a-glucan phosphorylases-stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and ortho-phosphate (arsenate) dependent reaction. Biochemistry 21, 6675-6684. doi:10.1021/bi00269a010
    • (1982) Biochemistry , vol.21 , pp. 6675-6684
    • Klein, H.W.1    Palm, D.2    Helmreich, E.J.M.3
  • 29
    • 0036197055 scopus 로고    scopus 로고
    • New routes to the synthesis of amylose-block-polystyrene rod-coil block copolymers
    • Loos, K., and Müller, A. H. E. (2002). New routes to the synthesis of amylose-block-polystyrene rod-coil block copolymers. Biomacromolecules 3, 368-373. doi:10.1021/bm0156330
    • (2002) Biomacromolecules , vol.3 , pp. 368-373
    • Loos, K.1    Müller, A.H.E.2
  • 30
    • 0031921128 scopus 로고    scopus 로고
    • Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening
    • Lorberth, R., Ritte, G., Willmitzer, L., and Kossmann, J. (1998). Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening. Nat. Biotechnol. 16, 473-477. doi:10.1038/nbt0598-473
    • (1998) Nat. Biotechnol , vol.16 , pp. 473-477
    • Lorberth, R.1    Ritte, G.2    Willmitzer, L.3    Kossmann, J.4
  • 31
    • 84928893327 scopus 로고    scopus 로고
    • Glyconanoparticles for colorimetric bioassays
    • Marin, M. J., Schofield, C. L., Field, R. A., and Russell, D. A. (2015). Glyconanoparticles for colorimetric bioassays. Analyst 140, 59-70. doi:10.1039/C4AN01466A
    • (2015) Analyst , vol.140 , pp. 59-70
    • Marin, M.J.1    Schofield, C.L.2    Field, R.A.3    Russell, D.A.4
  • 32
    • 23344448823 scopus 로고    scopus 로고
    • "Click chemistry" en route to pseudo-starch
    • Marmuse, L., Nepogodiev, S. A., and Field, R. A. (2005). "Click chemistry" en route to pseudo-starch. Org. Biomol. Chem. 3, 2225-2227. doi:10.1039/B504293C
    • (2005) Org. Biomol. Chem , vol.3 , pp. 2225-2227
    • Marmuse, L.1    Nepogodiev, S.A.2    Field, R.A.3
  • 33
    • 34247215644 scopus 로고    scopus 로고
    • Direct monitoring of both phosphorolysis and elongation of amylopectin catalyzed by phosphorylase on a 27-MHz quartz-crystal microbalance
    • Murakawa, A., Mori, T., and Okahata, Y. (2007). Direct monitoring of both phosphorolysis and elongation of amylopectin catalyzed by phosphorylase on a 27-MHz quartz-crystal microbalance. Chem. Lett. 36, 312-313. doi:10.1246/cl.2007.312
    • (2007) Chem. Lett , vol.36 , pp. 312-313
    • Murakawa, A.1    Mori, T.2    Okahata, Y.3
  • 34
    • 51249107951 scopus 로고    scopus 로고
    • Enzymatic a-glucosaminylation of maltooligosaccharides catalyzed by phosphorylase
    • Nawaji, M., Izawa, H., Kaneko, Y., and Kadokawa, J. (2008a). Enzymatic a-glucosaminylation of maltooligosaccharides catalyzed by phosphorylase. Carbohydr. Res. 343, 2692-2696. doi:10.1016/j.carres.2008.08.013
    • (2008) Carbohydr. Res , vol.343 , pp. 2692-2696
    • Nawaji, M.1    Izawa, H.2    Kaneko, Y.3    Kadokawa, J.4
  • 35
    • 46349098071 scopus 로고    scopus 로고
    • Enzymatic synthesis of a-D-xylosylated malto-oligosaccharides by phosphorylase-catalyzed xylosylation
    • Nawaji, M., Izawa, H., Kaneko, Y., and Kadokawa, J. I. (2008b). Enzymatic synthesis of a-D-xylosylated malto-oligosaccharides by phosphorylase-catalyzed xylosylation. J. Carbohydr. Chem. 27, 214-222. doi:10.1080/07328300802105340
    • (2008) J. Carbohydr. Chem , vol.27 , pp. 214-222
    • Nawaji, M.1    Izawa, H.2    Kaneko, Y.3    Kadokawa, J.I.4
  • 37
    • 8844239893 scopus 로고    scopus 로고
    • Kinetic studies of AMP-dependent phosphorolysis of amylopectin catalyzed by phosphorylase b on a 27 MHz quartz-crystal microbalance
    • Nishino, H., Murakawa, A., Mori, T., and Okahata, Y. (2004). Kinetic studies of AMP-dependent phosphorolysis of amylopectin catalyzed by phosphorylase b on a 27 MHz quartz-crystal microbalance. J. Am. Chem. Soc. 126, 14752-14757. doi:10.1021/ja046582k
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 14752-14757
    • Nishino, H.1    Murakawa, A.2    Mori, T.3    Okahata, Y.4
  • 38
    • 84961290433 scopus 로고    scopus 로고
    • Enzymatic synthesis using glycoside phosphorylases
    • O'Neill, E. C., and Field, R. A. (2015). Enzymatic synthesis using glycoside phosphorylases. Carbohydr. Res. 403, 23-37. doi:10.1016/j.carres.2014.06.010
    • (2015) Carbohydr. Res , vol.403 , pp. 23-37
    • O'Neill, E.C.1    Field, R.A.2
  • 39
    • 84888616193 scopus 로고    scopus 로고
    • Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materials
    • O'Neill, E. C., Rashid, A. M., Stevenson, C. E. M., Hetru, A.-C., Gunning, A. P., Rejzek, M., et al. (2014). Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materials. Chem. Sci. 5, 341-350. doi:10.1039/c3sc51829a
    • (2014) Chem. Sci , vol.5 , pp. 341-350
    • O'Neill, E.C.1    Rashid, A.M.2    Stevenson, C.E.M.3    Hetru, A.-C.4    Gunning, A.P.5    Rejzek, M.6
  • 40
    • 84868324053 scopus 로고    scopus 로고
    • Versatile high-resolution oligosaccharide microarrays for plant glycobiology and cell wall research
    • Pedersen, H. L., Fangel, J. U., McCleary, B., Ruzanski, C., Rydahl, M. G., Ralet, M.-C., et al. (2012). Versatile high-resolution oligosaccharide microarrays for plant glycobiology and cell wall research. J. Biol. Chem. 287, 39429-39438. doi:10.1074/jbc.M112.396598
    • (2012) J. Biol. Chem , vol.287 , pp. 39429-39438
    • Pedersen, H.L.1    Fangel, J.U.2    McCleary, B.3    Ruzanski, C.4    Rydahl, M.G.5    Ralet, M.-C.6
  • 41
    • 0000096811 scopus 로고
    • Extensive degradation of native starch granules by alpha-amylase from Aspergillus fumigatus
    • Planchot, V., Colonna, P., Gallant, D. J., and Bouchet, B. (1995). Extensive degradation of native starch granules by alpha-amylase from Aspergillus fumigatus. J. Cereal Sci. 21, 163-171. doi:10.1016/0733-5210(95)90032-2
    • (1995) J. Cereal Sci , vol.21 , pp. 163-171
    • Planchot, V.1    Colonna, P.2    Gallant, D.J.3    Bouchet, B.4
  • 43
    • 33745613836 scopus 로고    scopus 로고
    • a-D-Glucan-based dendritic nanoparticles prepared by in vitro enzymatic chain extension of glycogen
    • Putaux, J. L., Potocki-Veronese, G., Remaud-Simeon, M., and Buleon, A. (2006). a-D-Glucan-based dendritic nanoparticles prepared by in vitro enzymatic chain extension of glycogen. Biomacromolecules 7, 1720-1728. doi:10.1021/bm050988v
    • (2006) Biomacromolecules , vol.7 , pp. 1720-1728
    • Putaux, J.L.1    Potocki-Veronese, G.2    Remaud-Simeon, M.3    Buleon, A.4
  • 44
    • 66149118572 scopus 로고    scopus 로고
    • Spatiotemporal profiling of starch biosynthesis and degradation in the developing barley grain
    • Radchuk, V. V., Borisjuk, L., Sreenivasulu, N., Merx, K., Mock, H.-P., Rolletschek, H., et al. (2009). Spatiotemporal profiling of starch biosynthesis and degradation in the developing barley grain. Plant Physiol. 150, 190-204. doi:10.1104/pp.108.133520
    • (2009) Plant Physiol , vol.150 , pp. 190-204
    • Radchuk, V.V.1    Borisjuk, L.2    Sreenivasulu, N.3    Merx, K.4    Mock, H.-P.5    Rolletschek, H.6
  • 45
    • 84885158803 scopus 로고    scopus 로고
    • A Bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night
    • Ruzanski, C., Smirnova, J., Rejzek, M., Cockburn, D., Pedersen, H. L., Pike, M., et al. (2013). A Bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night. J. Biol. Chem. 288, 28581-28598. doi:10.1074/jbc.M113.497867
    • (2013) J. Biol. Chem , vol.288 , pp. 28581-28598
    • Ruzanski, C.1    Smirnova, J.2    Rejzek, M.3    Cockburn, D.4    Pedersen, H.L.5    Pike, M.6
  • 46
    • 84861058714 scopus 로고    scopus 로고
    • Gold nanoparticles in chemical and biological sensing
    • Saha, K., Agasti, S. S., Kim, C., Li, X., and Rotello, V. M. (2012). Gold nanoparticles in chemical and biological sensing. Chem. Rev. 112, 2739-2779. doi:10.1021/cr2001178
    • (2012) Chem. Rev , vol.112 , pp. 2739-2779
    • Saha, K.1    Agasti, S.S.2    Kim, C.3    Li, X.4    Rotello, V.M.5
  • 47
    • 79954421079 scopus 로고    scopus 로고
    • Progress in Arabidopsis starch research and potential biotechnological applications
    • Santelia, D., and Zeeman, S. C. (2011). Progress in Arabidopsis starch research and potential biotechnological applications. Curr. Opin. Biotechnol. 22, 271-280. doi:10.1016/j.copbio.2010.11.014
    • (2011) Curr. Opin. Biotechnol , vol.22 , pp. 271-280
    • Santelia, D.1    Zeeman, S.C.2
  • 48
  • 50
    • 79551699226 scopus 로고    scopus 로고
    • The role of a-glucosidase in germinating barley grains
    • Stanley, D., Rejzek, M., Naested, H., Smedley, M., Otero, S., Fahy, B., et al. (2011). The role of a-glucosidase in germinating barley grains. Plant Physiol. 155, 932-943. doi:10.1104/pp.110.168328
    • (2011) Plant Physiol , vol.155 , pp. 932-943
    • Stanley, D.1    Rejzek, M.2    Naested, H.3    Smedley, M.4    Otero, S.5    Fahy, B.6
  • 51
    • 0000112493 scopus 로고
    • Degradation of native starch granules by barley a-glucosidases
    • Sun, Z., and Henson, C. A. (1990). Degradation of native starch granules by barley a-glucosidases. Plant Physiol. 94, 320-327. doi:10.1104/pp.94.1.320
    • (1990) Plant Physiol , vol.94 , pp. 320-327
    • Sun, Z.1    Henson, C.A.2
  • 52
    • 84934443691 scopus 로고    scopus 로고
    • Preparation of pH-responsive amphoteric Glycogen hydrogels by a-glucan phosphorylase-catalyzed successive enzymatic reactions
    • Takata, Y., Yamamoto, K., and Kadokawa, J. (2015). Preparation of pH-responsive amphoteric Glycogen hydrogels by a-glucan phosphorylase-catalyzed successive enzymatic reactions. Macromol. Chem. Phys. 216, 1415-1420. doi:10.1002/macp.201500151
    • (2015) Macromol. Chem. Phys , vol.216 , pp. 1415-1420
    • Takata, Y.1    Yamamoto, K.2    Kadokawa, J.3
  • 53
    • 84865050325 scopus 로고    scopus 로고
    • An expedient enzymatic route to isomeric 2-, 3-and 6-monodeoxy-monofluoro-maltose derivatives
    • Tantanarat, K., Rejzek, M., O'Neill, E., Ruzanski, C., Hill, L., Fairhurst, S. A., et al. (2012). An expedient enzymatic route to isomeric 2-, 3-and 6-monodeoxy-monofluoro-maltose derivatives. Carbohydr. Res. 358, 12-18. doi:10.1016/j.carres.2012.05.026
    • (2012) Carbohydr. Res , vol.358 , pp. 12-18
    • Tantanarat, K.1    Rejzek, M.2    O'Neill, E.3    Ruzanski, C.4    Hill, L.5    Fairhurst, S.A.6
  • 54
    • 79952146837 scopus 로고    scopus 로고
    • In situ tracking of enzymatic breakdown of starch granules by synchrotron UV fluorescence microscopy
    • Tawil, G., Jamme, F., Refregiers, M., Vikso-Nielsen, A., Colonna, P., and Buleon, A. (2011). In situ tracking of enzymatic breakdown of starch granules by synchrotron UV fluorescence microscopy. Anal. Chem. 83, 989-993. doi:10.1021/ac1027512
    • (2011) Anal. Chem , vol.83 , pp. 989-993
    • Tawil, G.1    Jamme, F.2    Refregiers, M.3    Vikso-Nielsen, A.4    Colonna, P.5    Buleon, A.6
  • 55
    • 79952814469 scopus 로고    scopus 로고
    • Starch biosynthesis in developing seeds
    • Tetlow, I. J. (2011). Starch biosynthesis in developing seeds. Seed Sci. Res. 21, 5-32. doi:10.1017/S0960258510000292
    • (2011) Seed Sci. Res , vol.21 , pp. 5-32
    • Tetlow, I.J.1
  • 57
    • 84863408669 scopus 로고    scopus 로고
    • Enzymatic a-glucuronylation of maltooligosaccharides using a-glucuronic acid 1-phosphate as glycosyl donor catalyzed by a thermostable phosphorylase from Aquifex aeolicus VF5
    • Umegatani, Y., Izawa, H., Nawaji, M., Yamamoto, K., Kubo, A., Yanase, M., et al. (2012). Enzymatic a-glucuronylation of maltooligosaccharides using a-glucuronic acid 1-phosphate as glycosyl donor catalyzed by a thermostable phosphorylase from Aquifex aeolicus VF5. Carbohydr. Res. 350, 81-85. doi:10.1016/j.carres.2011.12.022
    • (2012) Carbohydr. Res , vol.350 , pp. 81-85
    • Umegatani, Y.1    Izawa, H.2    Nawaji, M.3    Yamamoto, K.4    Kubo, A.5    Yanase, M.6
  • 58
    • 0026027970 scopus 로고
    • Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs
    • Visser, R. G. F., Somhorst, I., Kuipers, G. J., Ruys, N. J., Feenstra, W. J., and Jacobsen, E. (1991). Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs. Mole. Gen. Genet. 225, 289-296. doi:10.1007/bf00269861
    • (1991) Mole. Gen. Genet , vol.225 , pp. 289-296
    • Visser, R.G.F.1    Somhorst, I.2    Kuipers, G.J.3    Ruys, N.J.4    Feenstra, W.J.5    Jacobsen, E.6
  • 59
    • 0032480718 scopus 로고    scopus 로고
    • Chiral side-chain liquid-crystalline polymeric properties of starch
    • Waigh, T. A., Perry, P., Riekel, C., Gidley, M. J., and Donald, A. M. (1998). Chiral side-chain liquid-crystalline polymeric properties of starch. Macromolecules 31, 7980-7984. doi:10.1021/ma971859c
    • (1998) Macromolecules , vol.31 , pp. 7980-7984
    • Waigh, T.A.1    Perry, P.2    Riekel, C.3    Gidley, M.J.4    Donald, A.M.5
  • 60
    • 0000631320 scopus 로고
    • The enzymic synthesis and N.M.R. characterisation of specifically deoxygenated and fluorinated glycogens
    • Withers, S. G. (1990). The enzymic synthesis and N.M.R. characterisation of specifically deoxygenated and fluorinated glycogens. Carbohydr. Res. 197, 61-73. doi:10.1016/0008-6215(90)84130-m
    • (1990) Carbohydr. Res , vol.197 , pp. 61-73
    • Withers, S.G.1
  • 61
    • 70350469659 scopus 로고    scopus 로고
    • Developing and engineering enzymes for manufacturing amylose
    • Yanase, M., Takaha, T., and Kuriki, T. (2007). Developing and engineering enzymes for manufacturing amylose. J. Appl. Glycosci. 54, 125-131. doi:10.5458/jag.54.125
    • (2007) J. Appl. Glycosci , vol.54 , pp. 125-131
    • Yanase, M.1    Takaha, T.2    Kuriki, T.3


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