Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

References

• Ademark P, de Vries RP, Hagglund P, et al. (2001). Cloning and characterization of Aspergillus niger genes encoding an α-galactosidase and a β-mannosidase involved in galactomannan degradation. Eur J Biochem, 268, 2982–90
   PubMedGoogle Scholar
• Ademark P, Lundqvist J, Hägglund P, et al. (1999). Hydrolytic properties of a β-mannosidase purified from Aspergillus niger. J Biotechnol, 75, 281–9
   PubMed Web of Science ®Google Scholar
• Anagnostopoulos C, Courtois JE, Petek F. (1954). The transferring action of α-galactosidase from coffee. Bull Soc Chim Biol (Paris), 36, 1115–23
   PubMedGoogle Scholar
• André C, Spangenberg P, Gentil E, Rabiller C. (2001). In situ 19F NMR spectroscopy study of enzymatic transglycosylation reactions using α-D-aldohexopyranosyl fluorides as donors and acceptors. Tetrahedron Asymmetry, 12, 779–83
   Web of Science ®Google Scholar
• Anggraeni AA, Sakka M, Kimura T, et al. (2008). Characterization of Bacillus halodurans α-galactosidase Mel4A encoded by mel4A gene (BH2228). Biosci Biotechnol Biochem, 72, 2459–62
   PubMed Web of Science ®Google Scholar
• Anisha GS, John RP, Prema P. (2011). Substrate specificities and mechanism of action of multiple α-galactosidases from Streptomyces griseoloalbus. Food Chem, 124, 349–53
   Web of Science ®Google Scholar
• Anisha GS, Prema P. (2008). Reduction of non-digestible oligosaccharides in horse gram and green gram flours using crude α-galactosidase from Streptomyces griseoloalbus. Food Chem, 106, 1175–9
   Web of Science ®Google Scholar
• Anisha GS, Rojan PJ, Nicemol J, et al. (2008). Production and characterization of partially purified thermostable α-galactosidases from Streptomyces griseoloalbus for food industrial applications. Food Chem, 111, 631–5
   Web of Science ®Google Scholar
• Bakunina IYu, Nedashkovskaya OI, Balabanova LA, et al. (2013). Comparative analysis of glycoside hydrolases activities from phylogenetically diverse marine bacteria of the genus Arenibacter. Mar Drugs, 11, 1977–98
   PubMed Web of Science ®Google Scholar
• Bakunina IYu, Nedashkovskaya OI, Kim SB, et al. (2012). Diversity of glycosidase activities in the bacteria of the phylum Bacteroidetes isolated from marine algae. Microbiology, 81, 688–95
   Web of Science ®Google Scholar
• Bakunina IYu, Nedashkovskaya OI, Zvyagintseva TN, Shchipunov YA. (2006). Immobilization of α-Galactosidase inside hybrid silica nanocomposites containing polysaccharides. Russ J Appl Chem, 79, 827–32
   Web of Science ®Google Scholar
• Bakunina IYu, Sova VV, Nedashkovskaya OI, et al. (1998). α-Galactosidase of the marine bacterium Pseudoalteromonas sp. KMM 701. Biochemistry (Moscow), 63, 1209–15
   PubMed Web of Science ®Google Scholar
• Balabanova LA, Bakunina IYu, Nedashkovskaya OI, et al. (2010). Molecular characterization and therapeutic potential of a marine bacterium Pseudoalteromonas sp. KMM 701 α-galactosidase. Mar Biotechnol, 12, 111–20
   PubMed Web of Science ®Google Scholar
• Balasubramaniam K, Mathew D. (1986). Purification of α-galactosidase from coconut. Phytochemistry, 25, 1819–21
   Web of Science ®Google Scholar
• Banner DW, Bloomer AC, Petsko GA, et al. (1975). Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution: using amino acid sequence data. Nature, 255, 609–14
   PubMed Web of Science ®Google Scholar
• Barnett JE. (1971). An acid-galactosidase from the albumen gland of Helix aspersa. Comp Biochem Physiol B, 40, 585–92
   PubMed Web of Science ®Google Scholar
• Bayraktar H, Onal S. (2013). Concentration and purification of α-galactosidase from watermelon (Citrullus vulgaris) by three phase partitioning. Sep Pur Technol, 118, 835–41
   Web of Science ®Google Scholar
• Biely P, Puchart V, Cote GL. (2001). Enzymic α-galactosylation of a cyclic glucotetrasaccharide derived from alternan. Carbohydr Res, 332, 299–303
   PubMed Web of Science ®Google Scholar
• Bishop DF, Desnick RJ. (1981). Affinity purification of α-galactosidase A from human spleen, placenta, and plasma with elimination of pyrogen contamination. Properties of the purified spleenic enzyme compared to other forms. J Biol Chem, 256, 1307–16
   PubMed Web of Science ®Google Scholar
• Blücher A, Karlsson EN, Holst O. (2000). Substrate-dependent production and some properties of a thermostable α-galactosidase from Rhodothermus marinus. Biotechnol Lett, 22, 663–9
   Web of Science ®Google Scholar
• Bonnet V, Boyer C, Langlois V, et al. (2003). An efficient, regioselective and fast enzymatic glycosylation for cyclodextrins. Tetrahedron Lett, 44, 8987–9
   Web of Science ®Google Scholar
• Boucher I, Vadeboncoeur C, Moineau S. (2003). Characterization of genes involved in the metabolism of α-galactosides by Lactococcus raffinolactis. Appl Environ Microbiol, 69, 4049–56
   PubMed Web of Science ®Google Scholar
• Brian T, Webb JA. (1977). Multiples forms of α-galactosidase in mature leaves of Cucurbita pepo. Phytochemistry, 16, 203–6
   Web of Science ®Google Scholar
• Brouns SJJ, Smits N, Wu H, et al. (2006). Identification of a novel α-galactosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. J Bacteriol, 188, 2392–9
   PubMed Web of Science ®Google Scholar
• Bruel L, Sulzenbacher G, Tison MC, et al. (2011). α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities. J Biol Chem, 286, 40814–23
   PubMed Web of Science ®Google Scholar
• Bryant R, Rao DR. (2000). Purification and characterization of α-galactoside from peanuts. J Food Biochem, 25, 27–98
   Google Scholar
• Buchanan-Wollaston V. (1997). The molecular biology of leaf senescence. J Exp Bot, 48, 181–99
   Web of Science ®Google Scholar
• Cantarel BL, Coutinho PM, Rancurel C, et al. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res, 37, D233–8
   PubMed Web of Science ®Google Scholar
• Cao Y, Yuan T, Shi P, et al. (2010). Properties of a novel α-galactosidase from Streptomyces sp. S27 and its potential for soybean processing. Enzyme Microb Technol, 47, 305–12
   Web of Science ®Google Scholar
• Casali M, Tarantini L, Riva S, et al. (2002). Explotation of a library of α-galactosidases for the synthesis of building blocks for glycopolymers. Biotechnol Bioneng, 77, 105–10
   PubMed Web of Science ®Google Scholar
• Cavazzoni V, Adami A, Craveri R. (1987). α-Galactosidase from the yeast Candida javanica. Appl Microbiol Biotechnol, 26, 555–9
   Web of Science ®Google Scholar
• Cervera-Tison M, Tailford LE, Fuell C, et al. (2012). Functional analysis of family GH-36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont. App Environ Microbiol, 78, 7720–32
   PubMed Web of Science ®Google Scholar
• Chakladar S, Cheng L, Choi M, et al. (2011). Mechanistic evaluation of MelA α-galactosidase from Citrobacter freundii: a family 4 glycosyl hydrolase in which oxidation is rate-limiting. Biochemistry, 50, 4298–308
   PubMed Web of Science ®Google Scholar
• Chien SF, Chen SH, Chien MY. (2008). Cloning, expression, and characterization of rice α-galactosidase. Plant Mol Biol Rep, 26, 213–24
   Web of Science ®Google Scholar
• Chien SF, Lin-Chu M. (1991). The conversion of group B red blood cells into group O by an α-galactosidase from taro Colocacia esculenta. Carbohydr Res, 217, 191–200
   PubMed Web of Science ®Google Scholar
• Chinen I, Nakamura T, Fukuda N. (1981). Purification and properties of α-galactosidase from immature stalks of Saccharum officinarum (sugar cane). J Biochem, 90, 1453–61
   PubMed Web of Science ®Google Scholar
• Chrost B, Daniel A, Krupinska K. (2004). Regulation of α-galactosidase gene expression in primary foliage leaves of barley (Hordeum vulgare L.) during dark-induced senescence. Planta, 218, 886–9
   PubMed Web of Science ®Google Scholar
• Civas A, Eberhard R, Le Dizet P, Petek F. (1984). Glycosidases induced in Aspergillus tamarii mycelial α-D-galactosidases. Biochem J, 219, 849–55
   PubMed Web of Science ®Google Scholar
• Clark NE, Garman SC. (2009). The 1,9 Å structure of human α-N-acetylgalactosaminidase: the molecular basis of Schindler and Kanzaki diseases. J Mol Biol, 393, 435–47
   PubMed Web of Science ®Google Scholar
• Cobucci-Ponzano B, Zorzetti C, Strazzulli A, et al. (2011). A novel α-D-galactosynthase from Thermotoga maritima converts β-D-galactopyranosyl azide to α-galacto-oligosaccharides. Glycobiology, 21, 448–56
   PubMed Web of Science ®Google Scholar
• Comfort DA, Bobrov KS, Ivanen DR, et al. (2007). Biochemical analysis of Thermotoga maritima GH-36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry, 46, 3319–30
   PubMed Web of Science ®Google Scholar
• Coombs J, Brenchley JE. (2000). Characterization of two new glycosyl hydrolases from the lactic acid bacterium Carnobacterium piscicola strain BA. Appl Environ Microbiol, 67, 5094–9
   Web of Science ®Google Scholar
• Corchero JL, Mendoza R, Miralles NF, et al. (2012). Enzymatic characterization of highly stable human α-galactosidase A displayed on magnetic particles. Biochem Eng J, 67, 20–7
   Web of Science ®Google Scholar
• Courtois JE, Petek F. (1957). Obtainment of epimelibiose by the transferase action of α-galactosidase. Bull Soc Chim Biol, 39, 715–23
   PubMedGoogle Scholar
• Coutinho PM, Henrissat B. (1999). Carbohydrate-active enzymes: an integrated database approach. In: Gilbert HJ, Davies G, Henrissat B, Svensson B, eds. Recent advances in carbohydrate bioengineering. Cambridge: The Royal Society of Chemistry, 3–12
   Google Scholar
• Crossman L, Dow JM. (2004). Biofilm formation and dispersal in Xanthomonas campestris. Microbes Infect, 6, 623–9
   PubMed Web of Science ®Google Scholar
• Davey ME, O'Toole GA. (2000). Microbial biofilms: from ecology to molecular genetics. Microbiol Mol Biol Rev, 64, 847–67
   PubMed Web of Science ®Google Scholar
• Davis MO, Hata DJ, Johnson SA, et al. (1996). Cloning, expression and characterization of a blood group B active recombinant α-D-galactosidase from soybean (Glycine max). Biochem Mol Biol Intern, 39, 471–85
   PubMedGoogle Scholar
• de Vries RP, van den Broeck HC, Deckers E, et al. (1999). Differential expression of three α-galactosidase genes and a single β-galactosidase gene from Aspergillus niger. Appl Environ Microbiol, 65, 2453–60
   PubMed Web of Science ®Google Scholar
• Dean KJ, Sweeley CC. (1979). Studies on human liver α-galactosidases. III. Partial characterization of carbohydrate-binding specificities. J Biol Chem, 254, 10006–10
   PubMed Web of Science ®Google Scholar
• Delente J, Johnson JH, Kuo MJ, et al. (1974). Production of a new thermostable neutral α-galactosidase from a strain of Bacillus stearothermophilus. Biotechnol Bioeng, 16, 1227–43
   PubMed Web of Science ®Google Scholar
• Demirev PA. (2013). Dried blood spots: analysis and applications. Anal Chem, 85, 779–89
   PubMed Web of Science ®Google Scholar
• Dey PM, Patel S, Brownleader MD. (1993). Induction of α-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum. Biotechnol Appl Biochem, 17, 361–71
   PubMed Web of Science ®Google Scholar
• Di Stefano M, Miceli E, Gotti S, et al. (2007). The effect of oral α-D-galactosidase on intestinal gas production and gas related symptoms. Dig Dis Sci, 52, 78–83
   PubMed Web of Science ®Google Scholar
• Dickmanns A, Ballschmiter M, Liebl W, Ficner R. (2006). Structure of the novel α-amylase AmyC from Thermotoga maritima. Acta Cryst, D62, 262–70
   Google Scholar
• Ensor L, Stosz S, Weiner R. (1999). Expression of multiple complex polysaccharide-degrading enzyme systems by marine bacterium strain 2-40. J Ind Microbiol Biotechnol, 23, 123–6
   PubMed Web of Science ®Google Scholar
• Feldt-Rasmussen U, Rasmussen AK, Mersebach H, et al. (2002). Fabry disease a metabolic disorder with a challenge for endocrinologists. Horm Res, 58, 259–65
   PubMed Web of Science ®Google Scholar
• Fernandez-Leiro R, Pereira-Rodríguez A, Cerdan ME, et al. (2010). Structural analysis of Saccharomyces cerevisiae α-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH-27 glycosidases. J Biol Chem, 285, 28020–33
   PubMed Web of Science ®Google Scholar
• Feurtado JA, Banik M, Bewley JD. (2001). The cloning and characterization of α-galactosidase present during and following germination of tomato (Lycopersicon esculentum) seed. J Exp Bot, 52, 1239–49
   PubMed Web of Science ®Google Scholar
• Filho M, Pessela BC, Mateo C, et al. (2008). Immobilization-stabilization of an α-galactosidase from Thermus sp. strain T2 by covalent immobilization on highly activated supports: selection of the optimal immobilization strategy. Enzyme Microb Technol, 42, 265–71
   Web of Science ®Google Scholar
• Fong JCN, Syed KA, Klose KE, Yildiz FH. (2010). Role of Vibrio polysaccharide (vps) genes in VPS production, biofilm formation and Vibrio cholerae pathogenesis. Microbiology, 156, 2757–69
   PubMed Web of Science ®Google Scholar
• Fredslund F, Hachem M, Larsen RJ, et al. (2011). Crystal structure of α-galactosidase from Lactobacillus acidophilus NCFM: insight into tetramer formation and substrate binding. J Mol Biol, 412, 466–80
   PubMed Web of Science ®Google Scholar
• Frias J, Price KR, Fenwick CL, et al. (1996). Improved method for the analysis of α-galactosides in pea seeds by capillary zone electrophoresis. Comparison with high-performance liquid chromatography triple-pulsed amperometric detection. J Chromatogr A, 719, 213–19
   PubMed Web of Science ®Google Scholar
• Fridjonsson O, Watzlawick H, Mattes R. (2000). The structure of the α-galactosidase gene loci in Thermus brockianus ITI 360 and Thermus thermophilus TH125. Extremophiles, 4, 23–33
   PubMed Web of Science ®Google Scholar
• Fujiki Y, Ito M, Nishida I, Watanabe A. (2000). Multiple signalling pathways in gene expression during sugar starvation: pharmacological analysis of din gene expression in suspension-cultured cells of Arabidopsis. Plant Physiol, 124, 1139–47
   PubMed Web of Science ®Google Scholar
• Fujimoto Z, Kaneko S, Kim WD, et al. (2009). The tetramer structure of the glycoside hydrolase family 27 α-galactosidase I from Umbelopsis vinacea. Biosci Biotechnol Biochem, 73, 2360–4
   PubMed Web of Science ®Google Scholar
• Fujimoto Z, Kaneko S, Momma M, et al. (2003). Crystal structure of rice α-galactosidase complexed with D-galactose. J Biol Chem, 278, 20313–18
   PubMed Web of Science ®Google Scholar
• Galas E, Miszkiewicz H. (1996). Purification and some properties of α-galactosidase from Mortierella vinacea IBT-3. Acta Microbiol Pol, 45, 143–54
   Google Scholar
• Galili U. (2005). The α-Gal epitope and the anti-Gal antibody in xenotransplantation and in cancer immunotherapy. Immunol Cell Biol, 83, 674–86
   PubMed Web of Science ®Google Scholar
• Galperin MY, Fernandez-Suarez XM. (2012). The 2012 Nucleic acids research database issue and the online molecular biology database collection. Nucleic Acids Res, 40, D1–8
   PubMed Web of Science ®Google Scholar
• Garman SC, Garboczi DN. (2004). The molecular defect leading to Fabry disease: structure of human α-galactosidase. J Mol Biol, 337, 319–35
   PubMed Web of Science ®Google Scholar
• Garman SC, Hannick L, Zhu A, Garboczi DN. (2002). The 1,9 Å structure of α-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. Structure, 10, 425–34
   PubMed Web of Science ®Google Scholar
• Gebus C, Cottin C, Randriantsoa M, et al. (2012). Synthesis of α-galactosyl epitopes by metabolically engineered Escherichia coli. Carbohydr Res, 361, 83–90
   PubMed Web of Science ®Google Scholar
• Gloster TM, Turkenburg JP, Potts JR, et al. (2008). Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol, 15, 1058–67
   PubMed Web of Science ®Google Scholar
• Goldstein J. (1989). Conversion of ABO blood groups. Transfus Med Rev, 3, 206–12
   PubMedGoogle Scholar
• Goldstein J. inventor. (1984). Enzymatic conversion of red cells for transfusion. US Patent 4,427,777
   Google Scholar
• Golubev AM, Nagem RAP, Brandão NJR, et al. (2004). Crystal structure of α-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism. J Mol Biol, 339, 413–22
   PubMed Web of Science ®Google Scholar
• Gomes J, Gomes II, Terler K, et al. (2000). Optimisation of culture medium and conditions for alpha-1-arabinofuranosidase production by the extreme thermophilic eubacterium Rhodothermus marinus. Enzyme Microbial Technol, 27, 414–22
   PubMed Web of Science ®Google Scholar
• Gong F, Lu QS, You Y, et al. (2005). Preparation of transfusable human universal red blood cell with recombinant α-galactosidase. Zhongguo Shi Yan Xue Ye Xue Za Zhi, 13, 313–16
   PubMedGoogle Scholar
• Gote M, Umalkar H, Khan I, Khire J. (2004). Thermostable α-galactosidase from Bacillus stearothermophilus (NCIM 5146) and its application in the removal of flatulence causing factors from soymilk. Process Biochem, 39, 1723–9
   Web of Science ®Google Scholar
• Goulas T, Goulas A, Tzortzis G, Gibson GR. (2009). A novel α-galactosidase from Βifidobacterium bifidum with transgalactosylating properties: gene molecular cloning and heterologous expression. Appl Microbiol Biotechnol, 82, 471–7
   PubMed Web of Science ®Google Scholar
• Hardee JR, Montogomert TM, Jones WH. (2000). Chemistry and flatulence: an introductory enzyme experiment. J Chem Educ, 77, 498–500
   Web of Science ®Google Scholar
• Harpaz N, Flowers HM, Sharon N. (1974). Purification of coffee bean α-galactosidase by affinity chromatography. Biochem Biophys Acta, 341, 213–21
   PubMed Web of Science ®Google Scholar
• Harpaz N, Flowers HM, Sharon N. (1975). Studies on B-antigenic sites of human erythrocytes by use of coffee bean α-galactosidase. Arch Biochem Biophys, 170, 676–83
   PubMed Web of Science ®Google Scholar
• Hashimoto H, Katayama C, Goto M, Kitahata S. (1993). Purification and some properties of α-galactosidase from Candida guilliermondii H-404. Biosci Biotechnol Biochem, 57, 372–8
   PubMed Web of Science ®Google Scholar
• Henrissat B, Callebaut I, Fabrega S, et al. (1995). Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA, 92, 7090–4
   PubMed Web of Science ®Google Scholar
• Hernaiz MJ, Crout DHG. (2000). Immobilization/stabilization on Eupergit C of the β-galactosidase from B. circulans and an α-galactosidase from Aspergillus oryzae. Enzyme Microb Technol, 27, 26–32
   PubMed Web of Science ®Google Scholar
• Hobbs L, Mitra M, Phillips R, Smith D. (1996). The activity of blood type B specific exoglycosidase from Glycine max. Clin Chim Acta, 247, 7–21
   PubMed Web of Science ®Google Scholar
• Huang CH, Liu RS, Wu TS, Cheng WC. (2008). Structural establishment of polygalatenosides A and B by total synthesis. Tetrahedron Lett, 49, 2895–8
   Web of Science ®Google Scholar
• Ishiguro M, Kaneko S, Kuno A, et al. (2001). Purification and characterization of the recombinant Thermus sp. strain T2 α-galactosidase expressed in Escherichia coli. Appl Environ Microbiol, 67, 1601–6
   PubMed Web of Science ®Google Scholar
• Ivanova EP, Bakunina IYu, Nedashkovskaya OI, et al. (1998). Incidence of marine microorganisms producing β-N-acetylglucosaminidases, α-galactosidases, and α-N-acetylgalactosaminidases. Russ J Mar Biol, 24, 365–72
   Google Scholar
• Jongkees SAK, Withers SG. (2014). Unusual enzymatic glycoside cleavage mechanisms. Acc Chem Res, 47, 226–35
   PubMed Web of Science ®Google Scholar
• Kang HC, Lee SH. (2001). Characteristics of an α-galactosidase associated with grape flesh. Phytochemistry, 58, 213–19
   PubMed Web of Science ®Google Scholar
• Kaplan JB, Meyenhofer MF, Fine DH. (2003). Biofilm growth and detachment of Actinobacillus actinomycetemcomitans. J Bacteriol, 185, 1399–404
   PubMed Web of Science ®Google Scholar
• Kawamura S, Kagawa-ken T, Kasai T, et al. (1971). Rapid microbiological production of alpha-galactosidase. US Patent 3,562,113
   Google Scholar
• Keates SE, Loewus F, Helms GL, Zink D. (1998). 5-O-(α-D-galactopyranosyl)-D-glycerol-pent-2-enono-1,4 lactone: characterization in the oxalate-producing fungus, Sclerotinia sclerotiorum. Phytochemistry, 49, 2397–401
   PubMed Web of Science ®Google Scholar
• Keller F, Pharr DM. (1996). Metabolism of carbohydrates in sink and sources: galactosyl-sucrose oligosaccharides. In: Zamski E, Schaffer AA, eds. Photoassimilate distribution in plants and crops. New York: Marcel Dekker, 157–83
   Google Scholar
• Kim WD, Kaneko S, Park GG, et al. (2003). Purification and characterization of α-galactosidase from sunflower seeds. Biotechnol Lett, 25, 353–8
   PubMed Web of Science ®Google Scholar
• Kim WD, Kobayashi O, Kaneko S, et al. (2002). α-Galactosidase from cultured rice (Oryza sativa L. var. Nipponbare) cells. Phytochemistry, 61, 621–30
   PubMed Web of Science ®Google Scholar
• Kitahata S, Hara K, Fujitya K, et al. (1992). Synthesis of 6-O-α-galactosyl α-cyclodextrin by coffee bean α-galactosidase. Biosci Biotechnol Biochem, 56, 1518–19
   PubMed Web of Science ®Google Scholar
• Koizumi K, Tanimoto T, Okada Y, et al. (1995). Isolation and characterization of novel heterogeneous branched cyclomalto-oligosaccharidess (cyclodextrins) produced by transgalactosylation with α-galactosidase from coffee bean. Carbohydr Res, 278, 129–42
   PubMed Web of Science ®Google Scholar
• Koshland DEJ. (1953). Stereochemistry and the mechanism of enzymatic reactions. Biol Rev Camb Phil Soc, 28, 416–36
   Web of Science ®Google Scholar
• Krieger N, Steiner W, Mitchell D. (2004). Foreword, Frontiers in biocatalysis. Food Technol Biotechnol, 42, 219–21
   Web of Science ®Google Scholar
• Kronzer F, Schuerch C. (1974). Use of positively charged leaving groups in the synthesis of α-D-linked galactosides. Attempted synthesis of 3-O-α-D-(galactopyranosyl)-D-galactose. Carbohydr Res, 33, 273–80
   Web of Science ®Google Scholar
• Kruskall MS, AuBuchon JP, Anthony KY, et al. (2000). Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O. Transfusion, 40, 1290–8
   PubMed Web of Science ®Google Scholar
• Kuo JY, Goldstein J. (1983). α-Galactosidase immobilized on a soluble polymer. Enzyme Microb Technol, 5, 285–90
   Web of Science ®Google Scholar
• Lemieux RU, Driguez H. (1975). The chemical synthesis of 2-O-(α-L-fucopyranosyl)-3-O-α-D-(galactopyranosyl)-D-galactose. The terminal structure of the blood-group B antigenic determinant. J Am Chem Soc, 97, 4069–75
   PubMed Web of Science ®Google Scholar
• Li H, Li Q, Cai MS, Li ZJ. (2000). Synthesis of galactosyl and lactosyl derivatives as potential anti metastasis compounds. Carbohydr Res, 328, 611–15
   PubMed Web of Science ®Google Scholar
• Li YT, Li Sc. (1999). Enzymatic hydrolysis of glycosphingolipids. Anal Biochem, 273, 1–11
   PubMed Web of Science ®Google Scholar
• Liljestroml PL, Liljestrom P. (1987). Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12. Nucleic Acids Res, 15, 2215–20
   Google Scholar
• Linden JC. (1982). Immobilized α-d-galactosidase in the sugar beet industry. Enzyme Microb Technol, 4, 130–6
   Web of Science ®Google Scholar
• Liu QP, Sulzenbacher G, Yuan H, et al. (2007). Bacterial glycosidases for the production of universal red blood cells. Nat Biotechnol, 25, 454–64
   PubMed Web of Science ®Google Scholar
• Liu QP, Yuan H, Bennett EP, et al. (2008). Identification of a GH-110 subfamily of α-1,3-galactosidases, novel enzymes for removal of the α3Gal xenotransplantation antigen. J Biol Chem, 283, 8545–54
   PubMed Web of Science ®Google Scholar
• Luonteri E, Alatalo E, Siika-Aho M, et al. (1998). α-galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI. Biotechnol Appl Biochem, 28, 179–88
   PubMed Web of Science ®Google Scholar
• Mai-Prochnow A. (2006). Autolysis in the development and dispersal of biofilms formed by the marine bacterium Pseudoalteromonas tunicate. PhD thesis, School of Biotechnology and Biomolecular Sciences, Faculty of Science, The University of New South Wales, Sydney, Australia
   Google Scholar
• Malhotra OP, Dey PM. (1967). Purification and physical properties of sweet almond α-galactosidase. Biochem J, 103, 508–13
   PubMed Web of Science ®Google Scholar
• Margolles-Clark E, Tenkanen M, Luonteri E, Penttilä M. (1996). Three α-galactosidase genes of Trichoderma reesei cloned by expression in yeast. Eur J Biochem, 240, 104–11
   PubMedGoogle Scholar
• Marraccini P, Rogers WJ, Caillet V, et al. (2005). Biochemical and molecular characterization of α-D-galactosidase from coffee beans. Plant Physiol Biochem, 43, 909–20
   PubMed Web of Science ®Google Scholar
• Martinez-Villaluenga C, Frias J, Vidal-Valverde CN. (2005). Raffinose family oligosaccharides and sucrose contents in 13 Spanish lupin cultivars. Food Chem, 91, 645–9
   Web of Science ®Google Scholar
• Martinez-Villaluenga C, Frias J, Vidal-Valverde CN. (2006). Functiona lupin seeds (Lupinus albus L. and Lupinus luteus L.) after extraction of a-galactosides. Food Chem, 98, 219–99
   Web of Science ®Google Scholar
• Martinez-Villaluenga C, Frias J, Vidal-Valverde CN. (2008). α-Galactosides: antinutritional factors or functional ingredients? Crit Rev Food Sci Nutr, 48, 301–16
   PubMed Web of Science ®Google Scholar
• Matsuo I, Fujimoto H, Isomura M, Katsumi A. (1997). Chemoenzymatic synthesis of Gal-α-1,3-gal, Gal-α-1,3-β1,4GlcNAc, and their PEG-conjugates. Bioorg Med Chem, 7, 255–8
   Web of Science ®Google Scholar
• Meier H, Reid JSG. (1982). Reserve polysaccharides other than starch in higher plants. In: Loewus FA, Tanner W, eds. Encyclopaedia of plant physiology. Berlin, Germany: Springer Verlag, 418–71
   Google Scholar
• Merceron R, Foucault M, Haser R, et al. (2012). The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by X-ray crystallography and mutational studies. J Biol Chem, 287, 39642–52
   PubMed Web of Science ®Google Scholar
• Morley TJ, Willis LM, Whitfield C, et al. (2009). A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase. J Biol Chem, 284, 17404–10
   PubMed Web of Science ®Google Scholar
• Muiznieks I, Rostoks N, Schmitt R. (1999). Efficient control of raf gene expression by CAP and two Raf repressors that bend DNA in opposite directions. Biol Chem, 380, 19–29
   PubMed Web of Science ®Google Scholar
• Mulimani VH, Dhananjay K. (2007). Immobilized α-galactosidase in the Biochemistry laboratory. J Chem Ed, 84, 1974–5
   Web of Science ®Google Scholar
• Nagao Y, Nakada T, Imoto M, et al. (1988). Purification and analysis of the structure of α-galactosidase from Escherichia coli. Biochem Biophys Res Commun, 151, 236–41
   PubMed Web of Science ®Google Scholar
• Naumoff DG. (2004). Phylogenetic analysis of α-gactosidases of GH-27 famiy. Mol Biol (Engl. Transl.), 38, 388–99
   Web of Science ®Google Scholar
• Naumoff DG. (2005). GH-97 is a new family of glycoside hydrolases, which is related to the α-galactosidase superfamily. BMC Genomics, 6, 112–24
   PubMed Web of Science ®Google Scholar
• Nieder V, Marx SP, Gutiérrez Gallego R, et al. (2003). Synthesis of nucleotide-activated disaccharides with β-galactosidase from Bacillus circulans and α-galactosidase from Bifidobacterium adolescentis. J Mol Cat B Enzyme, 21, 157–66
   Web of Science ®Google Scholar
• Ohtakara A, Mitsutomi M. (1987). Immobilization of thermostable α-galactosidase from Pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses. J Ferm Technol, 65, 493–8
   Web of Science ®Google Scholar
• Ohtakara M, Mitsutomi M, Uchida Y. (1984). Purification and enzymatic properties of α-galactosidase from Pycnoporus cinnabarinus. Agr Bio Chem, 48, 1319–27
   Web of Science ®Google Scholar
• Oishi K, Aida K. (1972). Blood group substance-degrading enzymes obtained from Streptomyces sp. Part II. Purification and characteristics of α-galactosidase from Streptomyces 9917S. Agric Biol Chem, 36, 578–87
   Web of Science ®Google Scholar
• Okada Y, Semma M, Ichikawa A. (2011). Physicochemical and biological properties of 2-O-α-D-galactosyl-cyclomalto-hexaose (α-cyclodextrin) and -cyclomaltoheptaose (β-cyclodextrin). Carbohydr Res, 346, 1018–22
   PubMed Web of Science ®Google Scholar
• Okutucu B, Celem EB, Önal S. (2010). Immobilization of α-galactosidase on galactose-containing polymeric beads. Enzyme Microb Technol, 6, 200–5
   Web of Science ®Google Scholar
• Okuyama M, Kitamura M, Hondoh H, et al. (2009). Catalytic mechanism of retaining α-galactosidase belonging to glycoside hydrolase family 97. J Mol Biol, 392, 1232–41
   PubMed Web of Science ®Google Scholar
• Olsson ML, Hilla CA, de laVega H, et al. (2004). Universal red blood cells-enzymatic conversion of blood group A and B antigens. Transf Clin Biol, 11, 33–9
   PubMed Web of Science ®Google Scholar
• Opazo R, Ortuzar F, Navarrete P, et al. (2012). Reduction of soybean meal non-starch polysaccharides and α-galactosides by solid-state fermentation using cellulolytic bacteria obtained from different environments. PLoS One, 7, 1–10, e44783
   Web of Science ®Google Scholar
• Orskov I, Orskov F. (1973). Plasmid determined H2S character in E. coli and its relation to plasmid-carried raffinose fermentation and tetracycline resistance characters. J Gen Microbiol, 77, 487–99
   PubMedGoogle Scholar
• Pardee A. (1957). An inducible mechanism for accumulation of melibiose in E. coli. J Bacteriol, 73, 376–85
   PubMed Web of Science ®Google Scholar
• Pennycooke JC, Jones ML, Stushnoff C. (2004). Expression of an α-galactosidase gene in Petunia is upregulated during low-temperature deacclimation. J Amer Soc Hort Sci, 129, 491–6
   Web of Science ®Google Scholar
• Pessela BC, Mateo C, Filho M, et al. (2008). Stabilization of the quaternary structure of a hexameric α-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques. Process Biochem, 43, 193–8
   Web of Science ®Google Scholar
• Pisani A, Visciano B, Diez-Roux G, et al. (2012). Enzyme replacement therapy in patients with Fabry disease: state of art and review of the literature. Mol Gen Metab, 107, 267–75
   PubMed Web of Science ®Google Scholar
• Post-Beittenmiller MA, Hamilton RW, Hopper JE. (1984). Regulation of basal and induced levels of the MEL1 transcript in Saccharomyces cerevisiae. Mol Cell Biol, 4, 1238–45
   PubMed Web of Science ®Google Scholar
• Prashanth SJ, Mulimani VH. (2005). Soymilk oligosaccharide hydrolysis by Aspergillus oryzae α-galactosidase immobilized in calcium alginate. Process Biochem, 40, 1199–205
   Web of Science ®Google Scholar
• Prestidge LS, Pardee AB. (1965). A second permease for methyl-thio-β-D-galactoside in E. coli. Biochim Biophys Acta, 100, 591–3
   PubMed Web of Science ®Google Scholar
• Puchart V, Vrsanska M, Bhat MK, Biely P. (2000). Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus. Biochim Biophys Acta, 1524; 27–37
   Web of Science ®Google Scholar
• Rajan SS, Yang X, Collart F, et al. (2004). Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+-dependent phospho-α-glucosidase from Bacillus subtilis. Structure, 12, 1619–29
   PubMed Web of Science ®Google Scholar
• Rezende ST, Guimaraes VM, Rodrigues MC, Felix CR. (2005). Purification and characterization of an α-galactosidase from Aspergillus fumigatus. Braz Arch Biol Technol, 48, 195–202
   Web of Science ®Google Scholar
• Rice SA, Koh KS, Queck SY, et al. (2005). Biofilm formation and sloughing in Serratia marcescens are controlled by quorum sensing and nutrient cues. J Bacteriol, 187, 3477–85
   PubMed Web of Science ®Google Scholar
• Rigden DJ. (2002). Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13. FEBS Lett, 523, 17–22
   PubMed Web of Science ®Google Scholar
• Rosenow C, Maniar M, Trias J. (1999). Regulation of the α-galactosidase activity in Streptococcus pneumoniae: characterization of the raffinose utilization system. Genome Res, 9, 1189–97
   PubMed Web of Science ®Google Scholar
• Ruiz JMJ, Oβwald G, Petersen M, Fessner WD. (2001). The “natural strategy” for the glycosidase-assisted synthesis of simple glycosides. J Mol Cat B Enzym, 11, 189–97
   Web of Science ®Google Scholar
• Russell RRB, Aduse-Opoku BJ, Sutcliffe IC, et al. (1992). A binding protein dependent transport system in Streptococcus mutans responsible for multiple sugar metabolisms. J Biol Chem, 267, 4631–7
   PubMed Web of Science ®Google Scholar
• Ryu JH, Kim H, Beuchat LR. (2004). Attachment and biofilm formation by Escherichia coli O157:H7 on stainless steel as influenced by exopolysaccharide production, nutrient availability, and temperature. J Food Prot, 67, 2123–31
   PubMed Web of Science ®Google Scholar
• Saier MHJ, Chauvaux S, Cook GM, et al. (1996). Catabolite repression and inducer control in Gram-positive bacteria. Microbiology, 142, 217–30
   PubMed Web of Science ®Google Scholar
• Saini HS. (1988). Extractability and evaluation of α-galactosides of sucrose in leguminous seeds. Food Chem, 28, 149–57
   Web of Science ®Google Scholar
• Sau A, Panchadhayee R, Ghosh D, Misra AK. (2012). Synthesis of a tetrasaccharide analog corresponding to the repeating unit of the O-polysaccharide of Salmonella enterica O59: unexpected stereo outcome in glycosylation. Carbohydr Res, 352, 18–22
   PubMed Web of Science ®Google Scholar
• Schmid K, Schmitt R. (1976). Raffinose metabolism in Escherichia coli K 12. Purification and properties of a new α-galactosidase specified by a transmissible plasmid. Eur J Biochem, 67, 95–104
   PubMedGoogle Scholar
• Scigelova M, Crout DHG. (2000). Purification of α-galactosidase from Aspergillus niger for application in the synthesis of complex oligosaccharides. J Mol Cat B Enzym, 4–6, 175–81
   Web of Science ®Google Scholar
• Shankar SK, Praveen Kumar SK, Mulimani VH. (2011). Calcium alginate entrapped preparation of α-galactosidase: its stability and application in hydrolysis of soymilk galactooligosaccharides. J Ind Microbiol Biotechnol, 38, 1399–405
   PubMed Web of Science ®Google Scholar
• Shimamoto T, Shimamoto T, Xu XJ, et al. (2001). A cryptic melibiose transporter gene possessing a frameshift from Citrobacter freundii. J Biochem, 129, 607–13
   PubMed Web of Science ®Google Scholar
• Shiozaki M, Tashiro T, Koshin H, et al. (2010). Synthesis and biological activity of ester and ether analogues of α-galactosylceramide (KRN7000). Carbohydr Res, 345, 1663–84
   PubMed Web of Science ®Google Scholar
• Shivam K, Mishra SK. (2010). Purification and characterization of a thermostable α-galactosidase with transglycosylation activity from Aspergillus parasiticus MTCC-2796. Process Biochem, 45, 1088–93
   Web of Science ®Google Scholar
• Shnit-Orland M, Sivan A, Kushmaro A. (2012). Antibacterial activity of Pseudoalteromonas in the coral holobiont. Microb Ecol, 64, 851–9
   PubMed Web of Science ®Google Scholar
• Silvestroni A, Connes C, Sesma F, et al. (2002). Characterization of the melA locus for α-galactosidase in Lactobacillus plantarum. Appl Environ Microbiol, 68, 5464–71
   PubMed Web of Science ®Google Scholar
• Simerska P, Kuzma M, Monti D, et al. (2006). Unique transglycosylation potential of extracellular α-D-galactosidase from Talaromyces flavus. J Mol Cat B Enzym, 39, 128–34
   Web of Science ®Google Scholar
• Simerska P, Kuzma M, Pisvejcova A, et al. (2003). Application of selectively acylated glycosides for the α-galactosidase-catalyzed synthesis of disaccharides. Folia Microbiol, 48, 329–37
   PubMed Web of Science ®Google Scholar
• Singh N, Kayastha AM. (2012). Cicer α-galactosidase immobilization onto chitosan and Amberlite MB-150: optimization, characterization, and its applications. Carbohydr Res, 358, 61–6
   PubMed Web of Science ®Google Scholar
• Song D, Chang SKC. (2006). Enzymatic degradation of oligosaccharides in pinto bean flour. J Agric Food Chem, 54, 1296–301
   PubMed Web of Science ®Google Scholar
• Sou C-P, Ali ZM, Lazan H. (2006). Characterisation of an α-galactosidase with potential relevance to ripening related texture changes. Phytochemistry, 67, 242–54
   PubMed Web of Science ®Google Scholar
• Spangenberg P, Andrè C, Langlois V, et al. (2002). α-Galactosyl fluoride in transfer reactions mediated by the green coffee beans α-galactosidase in ice. Carbohydr Res, 337, 221–8
   PubMed Web of Science ®Google Scholar
• Spangenberg P, Chiffoleau-Giraud V, André C, et al. (1999). Probing the transferase activity of glycosidases by means of in situ NMR spectroscopy. Tetrahedron Asymmetry, 10, 2905–12
   Web of Science ®Google Scholar
• Subba RK, Pieringer RA. (1970). Metabolism of glyceride glycolipids-IV: enzymatic hydrolysis of monogalactosyl and digalactosyl diglycerides in rat brain. J Neurochem, 245, 2520–4
   Google Scholar
• Sumner-Smith M, Bozzato RP, Skipper N, et al. (1985). Analysis of the inducible MEL1 gene of Saccharomyces carlsbergensis and its secreted product, α-galactosidase (melibiase). Gene, 36, 333–40
   PubMed Web of Science ®Google Scholar
• Suzuki N, Khoo KH, Chen CM, et al. (2003). N-glycan structure of pigeon IgG. A major serum glycoprotein containing Galα-1,4Gal termini. J Biol Chem, 278, 46293–306
   PubMed Web of Science ®Google Scholar
• Taji T, Ohsumi C, Iuchi S, et al. (2002). Important roles of drought- and cold-inducible genes for galactinol synthase in stress tolerance in Arabidopsis thaliana. Plant J, 29, 417–26
   PubMed Web of Science ®Google Scholar
• Takami H, Nakasone K, Takaki Y, et al. (2000). Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. Nucleic Acids Res, 28, 4317–31
   PubMed Web of Science ®Google Scholar
• Tester RF, Al-Ghazzewi FH. (2013). Mannans and health, with a special focus on glucomannans. Food Res Int, 50, 384–91
   Web of Science ®Google Scholar
• Tippeswamy S, Mulimani VH. (2003). Enzymic degradation of raffinose family oligosaccharides in soymilk by immobilized α-galactosidase from Gibberella fujikuroi. Process Biochem, 38, 635–40
   Web of Science ®Google Scholar
• Trincone A, Giordano A. (2006). Glycosyl hydrolases and glycosyltransferases in the synthesis of oligosaccharides. Curr Org Chem, 10, 1163–93
   Web of Science ®Google Scholar
• Trincone A. (2013). Angling for uniqueness in enzymatic preparation of glycosides. Biomolecules, 3, 334–50
   PubMedGoogle Scholar
• Van Lieshout JFT, Verhees CH, Ettema TJG, et al. (2003). Identification and molecular characterization of a novel type of α-galactosidase from Pyrococcus furiosus. Biocatal Biotransform, 21, 243–52
   Web of Science ®Google Scholar
• van Schaik W, Top J, Riley DR, et al. (2010). Pyrosequencing-based comparative genome analysis of the nosocomial pathogen Enterococcus faecium and identification of a large transferable pathogenicity island. BMC Genomics, 11, 239
   PubMed Web of Science ®Google Scholar
• Varbanets LD, Malanchuka VM, Buglova TT, Kuhlmann RA. (2001). Penicillium sp. 23 α-galactosidase: purification and substrate specificity. Carbohydr Polym, 44, 357–63
   Web of Science ®Google Scholar
• Varrot A, Yip VLY, Li Y, et al. (2005). NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-β-D-glucosides. J Mol Biol, 346, 423–35
   PubMed Web of Science ®Google Scholar
• Vic G, Hastings JJ, Crout DHG. (1996). Glycosidase-catalyzed synthesis of glycosides by an improved procedure for reverse hydrolysis: application to the chemoenzymatic synthesis of galactopyranosyl-(1-4)-O-α-galactopyranoside derivatives. Tetrahedron Asymmetry, 7, 1973–84
   Web of Science ®Google Scholar
• Weignerova L, Hunkova Z, Kuzma M, Kren V. (2001). Enzymatic synthesis of three pNP-α-galactobiopyranosides: application of the library of fungal α-galactosidases. J Mol Cat B Enzym, 11, 219–24
   Web of Science ®Google Scholar
• Weignerova L, Sedmera P, Hunkova Z, et al. (1999). Enzymatic synthesis of iso-globotriose from partially protected lactose. Tetrahedron Lett, 40, 9297–9
   Web of Science ®Google Scholar
• Wong H, Hu C, Yeh H, et al. (1986). Production, purification and characterization of α-galactosidase from Monascus pilosus. Appl Environ Microbiol, 52, 1147–52
   PubMed Web of Science ®Google Scholar
• Yagi H, Yamamoto M, Yu SY, et al. (2010). N-glycosylation profiling of turtle egg yolk: expression of galabiose structure. Carbohydr Res, 345, 442–8
   PubMed Web of Science ®Google Scholar
• Yates AD, Morgan WTJ, Watkins WM. (1975). Linkage-specific α-D-galactosidases from Trichomonas foetus: characterization of the blood-group B-destroying enzyme as a 1,3-α-galactosidase and the blood-group P1-destroying enzyme as a 1,4-α-galactosidase. FEBS Lett, 60, 281–5
   PubMed Web of Science ®Google Scholar
• Yip VLY, Varrot A, Davies GJ, et al. (2004). An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 β-glycosidase from Thermotoga maritima. J Am Chem Soc, 126, 8354–5
   PubMed Web of Science ®Google Scholar
• Zaprometova OM, Ulezlo IV, Lakhtin VM. (1990). Structure and properties of Cephalosporium acremonium α-galactosidase. Glycoconj J, 7, 287–300
   PubMed Web of Science ®Google Scholar
• Zaprometova OM, Ulezlo IV. (1988). Isolation and purification of a mold α-galactosidase. Biotechnol Appl Biochem, 10, 233–46
   Google Scholar
• Zhang YP, Gong F, Bao GQ, et al. (2007). B to O erythrocyte conversion by the recombinant α-galactosidase. Chin Med J, 120, 1145–50
   PubMed Web of Science ®Google Scholar
• Zhao H, Lu L, Xiao M, et al. (2008). Cloning and characterization of a novel α-galactosidase from Bifidobacterium breve 203 capable of synthesizing Gal-α-1,4 linkage. FEMS Microbiol Lett, 285, 278–83
   PubMed Web of Science ®Google Scholar
• Zhifang G, Schaffer A. (1999). A novel alkaline α-galactosidase from melon fruit with a substrate preference for raffinose. Plant Physiol, 119, 979–98
   PubMed Web of Science ®Google Scholar
• Zhu A, Leng L, Monahan C, et al. (1996). Characterization of recombinant α-galactosidase for use in seroconversion from blood group B to O of human erythrocytes. Arch Biochem Biophys, 327, 324–9
   PubMed Web of Science ®Google Scholar