Abstract
We recently succeeded in the identification and purification of an interesting marine exo-α-glucosidase (EC 3.2.1.20) from the anaspidean mollusc Aplysia fasciata. The enzyme was characterized by good transglycosylation activity toward different acceptors using maltose as donor. High-yielding enzymatic α-glycosylation of pyridoxine using this marine enzyme is reported here; the reaction has been optimized, reaching 80% molar yield of products (pyridoxine monoglucosides 24 g/l; pyridoxine isomaltoside 35 g/l). High selectivity toward the 5′ position is observed for both monoglucoside and disaccharide formation. This is the first report describing the enzymatic production of pyridoxine isomaltoside.
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Andreotti G, Giordano A, Tramice A, Mollo E, Trincone A (2005a) Hydrolyses and transglycosylations performed by purified α-glucosidase of the marine mollusc Aplysia fasciata. J Biotechnol http://dx.doi.org/10.1016/j.jbiotec.2005.10.002
G Andreotti A Giordano A Tramice E Mollo A Trincone (2005) ArticleTitlePurification and characterization of a β-mannosidase from the marine anaspidean Aplysia fasciata J Biotechnol 119 26–35 Occurrence Handle10.1016/j.jbiotec.2005.06.003
Y Asano K Wada (2003) ArticleTitleRegioselective glucosylation of pyridoxine by microorganisms Biosci Biotechnol Biochem 67 499–507 Occurrence Handle10.1271/bbb.67.499
Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quatities of protien utilizing the principle of protein-dye binding. Anal Biochem 72, 248–254
T Carefoot (1987) ArticleTitleAplysia: its biology and ecology Oceanogr Mar Biol Ann Rev 25 284–290
A Giordano G Andreotti E Mollo A Trincone (2004) ArticleTitleTransglycosylation reactions performed by glycosyl hydrolases from the marine anaspidean mollusc Aplysia fasciata J Mol Cat B Enzym 30 51–59 Occurrence Handle10.1016/j.molcatb.2004.03.007
A Giordano A Tramice G Andreotti E Mollo A Trincone (2005) ArticleTitleEnzymatic synthesis and selective hydrolysis of O-β-d-galactopyranosides using a marine mollusc b-galactosidase Biorg Med Chem Lett 15 139–143 Occurrence Handle10.1016/j.bmcl.2004.10.016
T Joseph H Tsuge Y Suzuki DB McCormick (1996) ArticleTitlePyridoxine 4′-alpha- and 5′-alpha-d-glucosides are taken up and metabolized by isolated rat liver cells J Nutr 126 2899–2903
N Kato S Suyama M Shirokane M Kato T Kobayashi N Tsukagoshi (2002) ArticleTitleNovel α-glucosidase from Aspergillus nidulans with strong transglycosylation activity Appl Environ Microbiol 66 1250–1256 Occurrence Handle10.1128/AEM.68.3.1250-1256.2002
F Kawai H Yamada K Ogata (1971) ArticleTitleProperties of pyridoxine glucoside J Vitaminol 17 121–124
S Malà H Dvorakova R Hrabal B Kralova (1999) ArticleTitleTowards regioselective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity Carbohydr Res 322 209–218 Occurrence Handle10.1016/S0008-6215(99)00222-0
R Pagani R Leoncini L Terzuoli M Pizzichini E Marinello (1994) ArticleTitleThe regulation of alanine and aspartate aminotransferase by different aminothiols and by vitamin B-6 derivatives Biochim Biophys Acta 1204 250–256
P Pham W Zhang V Chen T Whitney J Yao D Froese AD Friesen JM Diakur W Haque (2003) ArticleTitleDesign and synthesis of novel pyridoxine 5′-phosphonates as potential antiischemic agents J Med Chem 46 3680–3687 Occurrence Handle10.1021/jm0300678
Y Suzuki K Uchida (1997) ArticleTitleFormation of β-galactosides of pyridoxine using Sporobolomyces singularis Methods Enzymol 280 71–77
Y Suzuki Y Doi K Uchida H Tsuge (1997) ArticleTitleEnzymatic preparation of pyridoxine 4′- and 5′-α-d-glucosides Methods Enzymol 280 66–71 Occurrence Handle10.1016/S0076-6879(97)80102-4
H Tsuge M Maeno T Hayakawa Y Suzuki (1996) ArticleTitleComparative study of pyridoxine-alpha, beta-glucosides, and phosphopyridoxyl-lysine as a vitamin B6 nutrient J Nutr Sci Vitaminol 42 377–386
P Venier A Pallavicini B Nardi ParticleDe G Lanfranchi (2003) ArticleTitleTowards a catalogue of genes transcribed in multiple tissues of Mytilus galloprovincialis Gene 314 29–40 Occurrence Handle10.1016/S0378-1119(03)00708-X
K Wada Y Asano (2003) ArticleTitleImprovement in 5′-position-selective glucosylation of pyridoxine by Verticillium dahliae TPU 4900 Biosci Biotechnol Biochem 67 508–516 Occurrence Handle10.1271/bbb.67.508
B Westerop (2003) ArticleTitleAbstracts of Marine Biotechnology: basics and applications Biomol Eng 20 37–82 Occurrence Handle10.1016/S1389-0344(03)00005-4
Acknowledgments
The authors wish to thank E. Pagnotta and R. D'Ambrosio for technical assistance, and S. Zambardino, D. Melck, and V. Mirra (NMR Service of Istituto di Chimica Biomolecolare, CNR, Pozzuoli, Italy). NMR spectra were obtained using a Bruker DPX-300 operating at 300 MHz, with a dual probe and/or on a Bruker Avance-400 operating at 400 MHz, using an inverse probe fitted with a gradient along the Z-axis. Dr. A. Tramice wishes to thank Centro Regionale di Competenza in Applicazioni Tecnologico-Industriali di Biomolecole e Biosistemi for a fellowship.
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Tramice, A., Giordano, A., Andreotti, G. et al. High-Yielding Enzymatic α-Glucosylation of Pyridoxine by Marine α-Glucosidase from Aplysia fasciata . Mar Biotechnol 8, 448–452 (2006). https://doi.org/10.1007/s10126-005-6144-4
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DOI: https://doi.org/10.1007/s10126-005-6144-4