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Ademark, P., Larsson, M., Tjerneld, F., Stalbrand, H. (2001) Multiple α-galactosidases from Aspergillus niger: purification, characterization and substrate specificities. Enzyme Microb. Technol. 29 , 441

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Acta Microbiologica et Immunologica Hungarica
Authors: Petra Havas, Szilárd Kun, Izabell Perger-Mészáros, Judit M. Rezessy-Szabó, and Quang D. Nguyen

Growth and metabolic activity of several new, human origin isolates of Bifidobacterium strains were investigated. All tested bifidobacteria strains were grown well on the native soymilk medium without any additional nutrients. The fermentation processes cultured with initial cell concentrations in 105–107 cfu/ml resulted in 108 cfu/ml after 8–12 h of incubation in soymilk, and were kept viable up to the end of fermentation (48 h). Volumetric productivities of B. bifidum B3.2, B. bifidum B7.1 and B. breve B9.14 were 1.6×1010 cfu/L.h, 4.5×1010 cfu/L.h and 7.6×109 cfu/L.h, respectively, whereas these values of B. lactis Bb-12 and B. longum Bb-46 probiotic strains were 2.7×109 cfu/L.h and 1.0×1010 cfu/L.h. The α-galactosidase activities were also detected in the intracellular fraction of the disrupted cells. Productions of lactic and acetic acids were in the range of 23–60 mmol/L and 2.4–5.6 mmol/L, respectively. Molar ratios of acetate to lactate in all tested strains varied from 0.05–0.1 that are very promising for further technological development of probiotic fermented soy-based food products.

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Orvosi Hetilap
Authors: Éva Rákóczi, Sándor Görögh, János Grubits, Melinda Erdős, Ferenc Garzuly, Katalin Hahn, Krisztina Bencsik, László Vécsei, Csilla Trinn, Éva Kristóf, Gábor Mogyorósy, Beáta Tóth, and László Maródi

807 Desnick, R. J.: Enzyme replacement therapy for Fabry disease: lessons from two α-galactosidase A orphan products and one FDA approval. Expert Opin. Biol. Ther., 2004, 4

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De vries, R. P., Van Den Broeck, H., Dekkers, E., Manzanares, P., De Graff, L. H., & Visser, J. (1999): Differential expression of three α-galactosidase gene from Aspergillus niger . Appl. Environ. Microbiol

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): Evaluation of α-galactosidase biosynthesis by Streptomyces griseoalbus in solid state fermentation . Lett. Appl. Microbiol. , 46 , 338 – 345 . Assamoi

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Acta Alimentaria
Authors: O. Velasco-González, S. Echavarría-Almeida, A. Pajarito, and E. San Martín-Martinez

3223 3227 Matella, N.J., Dolan, K.D., Stoeckle, A.W., Bennink, M.R., Lee, Y.S. & Uebersax, M.A. (2005): Use of hydration, germination, and α-galactosidase

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Acta Biologica Hungarica
Authors: András Kerchner, Judit Darók, Ivett Bacskay, Attila Felinger, Gábor Jakab, and Ágnes Farkas

. , Chen , L. Y. , Sun , H. ( 2012 ) Acidic α-galactosidase is the most abundant nectarin in floral nectar of common tobacco ( Nicotiana tabacum ) . Annals Bot. 109 , 735 – 745 .

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159 2070 2076 Donkor, O.N., Henriksson, A., Vasiljevic, T. & Shah, N.P. (2006): α-Galactosidase and proteolytic activity of

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detected in all tested strains at low or intermediate (2/5) levels ( Table 2 ). α-Galactosidase activity was found at a low level only in strain D. hansenii 161. N-acetyl-β-glucoaminidase activity was found at intermediate (2/5) level only in strain D

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