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Santos, C.R.D., De Giuseppe, P.O., De Souza, F.H.M., Zanphorlin, L.M., Domingous, M.N., Pirolla, R.A.S., Honorato, R.V., Tonoli, C.C.C., De Morais, M.A.B., De Matos Martin, V.P., Fonsecam, L.M., Büchli, F., De Oliveira, P.S.L., Gozzo, F.C. and Murakami, M.T. (2008) The Mechanism by Which a Distinguishing Arabinofuranosidase Can Cope with Internal Di-Substitutions in Arabinoxylans. Biotechnology for Biofuels, 11, Article No. 223.
https://doi.org/10.1186/s13068-018-1212-y

has been cited by the following article:

• TITLE: Cloning of an α-L-Arabinofuranosidase and Characterization of Its Action on Mono- and Di-Substituted Xylopyranosyl Units

  AUTHORS: Dominic W. S. Wong, Sarah Batt

  KEYWORDS: α-L-Arabinofuranosidase, Mono-Substituted Xylopyranosyl Unit, Di-Substituted Xylopyranosyl Unit, Arabinofuranosyl Xylooligosaccharides (AXOS)

  JOURNAL NAME: Advances in Enzyme Research, Vol.10 No.4, December 12, 2022

  ABSTRACT: An α-L-arabinofuranosidase (ARF) gene of 1503 bp was synthesized, subcloned into pET26b vector, and expressed in Escherichia coli. The enzyme was purified in active form, and consisted of 500 amino acid residues, corresponding to 55 kD based on SDS-PAGE. The affinity-purified protein was characterized using arabinofuranosyl xylooligosaccharides (AXOS) as substrates. The pH effect was investigated showing an optimum at pH 5.5. XaARF catalyzed the cleavage of arabinose at C3 of the xylopyranosyl unit efficiently if the arabinofuranosyl substitution was at the terminal compared to internal xylose units. The enzyme was able to act on di-substituted xylopyranosyl units with the first cleavage at C3 followed by C2 linkages.