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Peculiarities and applications of galactanolytic enzymes that act on type I and II arabinogalactans

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Abstract

Arabinogalactans (AGs) are branched galactans to which arabinose residues are bound as side chains and are widely distributed in plant cell walls. They can be grouped into two types based on the structures of their backbones. Type I AGs have β-1,4-galactan backbones and are often covalently linked to the rhamnogalacturonan-I region of pectins. Type II AGs have β-1,3-galactan backbones and are often covalently linked to proteins. The main enzymes involved in the degradation of AGs are endo-β-galactanases, exo-β-galactanases, and β-galactosidases, although other enzymes such as α-l-arabinofuranosidases, β-l-arabinopyranosidases, and β-d-glucuronidases are required to remove the side chains for efficient degradation of the polysaccharides. Galactanolytic enzymes have a wide variety of potential uses, including the bioconversion of AGs to fermentable sugars for production of commodity chemicals like ethanol, biobleaching of cellulose pulp, modulation of pectin properties, improving animal feed, and determining the chemical structure of AGs. This review summarizes our current knowledge about the biochemical properties and potential applications of AG-degrading enzymes.

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Acknowledgments

This research was partially supported by a grant-in-aid for scientific research (22580091) from the Japan Society for the Promotion of Science.

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  1. Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, 599-8531, Japan

    Tatsuji Sakamoto

  2. Department of Science and Technology on Food Safety, Faculty of Biology-Oriented Science and Technology, Kinki University, Wakayama, 649-6493, Japan

    Megumi Ishimaru

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Sakamoto, T., Ishimaru, M. Peculiarities and applications of galactanolytic enzymes that act on type I and II arabinogalactans. Appl Microbiol Biotechnol 97, 5201–5213 (2013). https://doi.org/10.1007/s00253-013-4946-2

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  • DOI: https://doi.org/10.1007/s00253-013-4946-2

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