References
- Saha BC. 2003. Hemicelluose bioconversion. J. Ind. Microbiol. Biotechnol. 30: 279-291. https://doi.org/10.1007/s10295-003-0049-x
- Hizukuri S. 1999. Nutritional and physiological functions and uses of L-arabinose. J. Appl. Glycosci. 46: 159-165. https://doi.org/10.5458/jag.46.159
- Seri K, Sanai K, Matsuo N, Kawakubo K, Xue C, Inoue S. 1996. ʟ-Arabinose selectively inhibits intestinal sucrase in an uncompetitive manner and suppresses glycemic response after sucrose ingestion in animals. Metabolism 45: 1368-1374. https://doi.org/10.1016/S0026-0495(96)90117-1
- Moon JS, Shin SY, Choi HS, Joo W, Cho SK, Li L, et al. 2015. In vitro digestion and fermentation properties of linear sugar-beet arabinan and its oligosaccharides. Carbohydr. Polym. 131: 50-56. https://doi.org/10.1016/j.carbpol.2015.05.022
- Numan MT, Bhosle NB. 2006. α-ʟ-Arabinofuranosidases: the potential applications in biotechnology. J. Ind. Microbiol. Biotechnol. 33: 247-260. https://doi.org/10.1007/s10295-005-0072-1
- Poria V, Saini JK, Singh S, Nain L, Kuhad RC. 2020. Arabinofuranosidases: Characteristics, microbial production, and potential in waste valorization and industrial applications. Bioresour. Technol. 304: 123019. https://doi.org/10.1016/j.biortech.2020.123019
- Lim YR, Yeom SJ, Kim YS, Oh DK. 2011. Synergistic production of L-arabinose from arabinan by the combined use of thermostable endo- and exo-arabinanases from Caldicellulosiruptor saccharolyticus. Bioresour. Technol. 102: 4277-4280. https://doi.org/10.1016/j.biortech.2010.12.039
- Park JM, Jang MU, Oh GW, Lee EH, Kang JH, Song YB, et al. 2015. Synergistic action modes of arabinan degradation by exo- and endo-arabinosyl hydrolases. J. Microbiol. Biotechnol. 25: 227-233. https://doi.org/10.4014/jmb.1411.11055
- Seiboth B, Metz B. 2011. Fungal arabinan and ʟ-arabinose metabolism. Appl. Microbiol. Biotechnol. 89: 1665-1673. https://doi.org/10.1007/s00253-010-3071-8
- Sa-Nogueira I, Nogueira TV, Soares S, de Lencastre H. 1997. The Bacillus subtilis ʟ-arabinose (ara) operon: nucleotide sequence, genetic organization and expression. Microbiology 143: 957-969. https://doi.org/10.1099/00221287-143-3-957
- Inacio JM, Correia IL, de Sa-Nogueira I. 2008. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis. Microbiology 154: 2719-2729. https://doi.org/10.1099/mic.0.2008/018978-0
- Shulami S, Raz-Pasteur A, Tabachnikov O, Gilead-Gropper S, Shner I, Shoham Y. 2011. The ʟ-arabinan utilization system of Geobacillus stearothermophilus. J. Bacteriol. 193: 2838-2850. https://doi.org/10.1128/JB.00222-11
- Kawaguchi H, Sasaki M, Vertès AA, Inui M, Yukawa H. 2009. Identification and functional analysis of the gene cluster for ʟ-arabinose utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75: 3419-3429. https://doi.org/10.1128/AEM.02912-08
- Shinozaki A, Hosokawa S, Nakazawa M, Ueda M, Sakamoto T. 2015. Identification and characterization of three Penicillium chrysogenum α-ʟ-arabinofuranosidases (PcABF43B, PcABF51C, and AFQ1) with different specificities toward arabino-oligosaccharides. Enzyme Microb. Technol. 73-74: 65-71. https://doi.org/10.1016/j.enzmictec.2015.04.003
- Bauer S, Vasu P, Persson S, Mort AJ, Somerville CR. 2006. Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls. Proc. Natl. Acad. Sci. USA 103: 11417-11422. https://doi.org/10.1073/pnas.0604632103
- Pouvreau L, Joosten R, Hinz SW, Gruppen H, Schols HA. 2011. Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans. Enzyme Microb. Technol. 48: 397-403. https://doi.org/10.1016/j.enzmictec.2011.01.004
- Ohta K, Fujii S, Higashida C. 2013. Characterization of a glycoside hydrolase family-51 α-ʟ-arabinofuranosidase gene from Aureobasidium pullulans ATCC 20524 and its encoded product. J. Biosci. Bioeng. 116: 287-292. https://doi.org/10.1016/j.jbiosc.2013.03.009
- Uesaka E, Sato M, Raiju M, Kaji A. 1978. α-ʟ-Arabinofuranosidase from Rhodotorula flava. J. Bacteriol. 133: 1073-1077. https://doi.org/10.1128/jb.133.3.1073-1077.1978
- Yanai T, Sato M. 2000. Purification and characterization of a novel α-ʟ-arabinofuranosidase from Pichia capsulata X91. Biosci. Biotechnol. Biochem. 64: 1181-1188. https://doi.org/10.1271/bbb.64.1181
- Fonseca C, Romao R, Rodrigues de Sousa H, Hahn-Hagerdal B, Spencer-Martins I. 2007. ʟ-Arabinose transport and catabolism in yeast. FEBS J. 274: 3589-3600. https://doi.org/10.1111/j.1742-4658.2007.05892.x
- Choo JH, Hong CP, Lim JY, Seo JA, Kim YS, Lee DW, et al. 2016. Whole-genome de novo sequencing, combined with RNA-Seq analysis, reveals unique genome and physiological features of the amylolytic yeast Saccharomycopsis fibuligera and its interspecies hybrid. Biotechnol. Biofuels 9: 246. https://doi.org/10.1186/s13068-016-0653-4
- Chi Z, Chi Z, Liu G, Wang F, Ju L, Zhang T. 2009. Saccharomycopsis fibuligera and its applications in biotechnology. Biotechnol. Adv. 27: 423-431. https://doi.org/10.1016/j.biotechadv.2009.03.003
- Lee DW, Hong CP, Kang HA. 2019. An effective and rapid method for RNA preparation from non-conventional yeast species. Anal. Biochem. 586: 113408. https://doi.org/10.1016/j.ab.2019.113408
- Dumbrepatil A, Park JM, Jung TY, Song HN, Jang MU, Han NS, et al. 2012. Structural analysis of α-ʟ-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity. J. Microbiol. Biotechnol. 22: 1724-1730. https://doi.org/10.4014/jmb.1208.08043
- Oh GW, Kang Y, Choi CY, Kang SY, Kang JH, Lee ML, et al. 2019. Detailed mode of action of arabinan-debranching α-ʟ-arabinofuranosidase GH51 from Bacillus velezensis. J. Microbiol. Biotechnol. 29: 37-43. https://doi.org/10.4014/jmb.1807.11035
- Beylot MH, McKie VA, Voragen AG, Doeswijk-Voragen CH, Gilbert HJ. 2001. The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity. Biochem. J. 358: 607-614. https://doi.org/10.1042/bj3580607
- Debeche T, Cummings N, Connerton I, Debeire P, O'Donohue MJ. 2000. Genetic and biochemical characterization of a highly thermostable α-ʟ-arabinofuranosidase from Thermobacillus xylanilyticus. Appl. Environ. Microbiol. 66: 1734-1736. https://doi.org/10.1128/AEM.66.4.1734-1736.2000
- Michlmayr H, Schümann C, Kulbe KD, del Hierro AM. 2011. Heterologously expressed family 51 α-ʟ-arabinofuranosidases from Oenococcus oeni and Lactobacillus brevis. Appl. Environ. Microbiol. 77: 1528-1531. https://doi.org/10.1128/AEM.01385-10
- Margolles A, de los Reyes-Gavilan CG. 2003. Purification and functional characterization of a novel α-ʟ-arabinofuranosidase from Bifidobacterium longum B667. Appl. Environ. Microbiol. 69: 5096-5103. https://doi.org/10.1128/AEM.69.9.5096-5103.2003
- Cartmell A, McKee LS, Peña MJ, Larsbrink J, Brumer H, Kaneko S et al. 2011. The structure and function of an arabinan-specific α-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases. J. Biol. Chem. 286: 15483-15495. https://doi.org/10.1074/jbc.M110.215962
- Michlmayr H, Hell J, Lorenz C, Bohmdorfer S, Rosenau T, Kneifel W. 2013. Arabinoxylan oligosaccharide hydrolysis by family 43 and 51 glycosidases from Lactobacillus brevis DSM 20054. Appl. Environ. Microbiol. 79: 6747-6754. https://doi.org/10.1128/AEM.02130-13
- Ichinose H, Yoshida M, Fujimoto Z, Kaneko S. 2008. Characterization of a modular enzyme of exo-1,5-α-ʟ-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893. Appl. Microbiol. Biotechnol. 80: 399-408. https://doi.org/10.1007/s00253-008-1551-x
- Linares-Pasten JA, Falck P, Albasri K, Kjellstrom S, Adlercreutz P, Logan DT et al. 2017. Three-dimensional structures and functional studies of two GH43 arabinofuranosidases from Weissella sp. strain 142 and Lactobacillus brevis. FEBS J. 284: 2019-2036. https://doi.org/10.1111/febs.14101
- Paes G, Skov LK, O'Donohue MJ, Remond C, Kastrup JS, Gajhede M et al. 2008. The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit. Biochemistry 47: 7441-7451. https://doi.org/10.1021/bi800424e
- Zietsman AJ, de Klerk D, van Rensburg P. 2011. Coexpression of α-ʟ-arabinofuranosidase and β-glucosidase in Saccharomyces cerevisiae. FEMS Yeast Res. 11: 88-103. https://doi.org/10.1111/j.1567-1364.2010.00694.x