Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

  • Martina Aulitto
  • Salvatore Fusco
  • Danila Limauro
  • Gabriella Fiorentino
  • Simonetta Bartolucci
  • Patrizia ContursiEmail author


Extremophilic microorganisms are valuable sources of enzymes for various industrial applications. In fact, given their optimal catalytic activity and operational stability under harsh physical and chemical conditions, they represent a suitable alternative to their mesophilic counterparts. For instance, extremophilic enzymes are important to foster the switch from fossil-based to lignocellulose-based industrial processes. Indeed, more stable enzymes are needed, because the conversion of the lignocellulosic biomass to a wide palette of value-added products requires extreme chemo-physical pre-treatments. Galactomannans are part of the hemicellulose fraction in lignocellulosic biomass. They are heteropolymers constituted by a β-1,4-linked mannan backbone substituted with side chains of α-1,6-linked galactose residues. Therefore, the joint action of different hydrolytic enzymes (i.e. β-mannanase, β-mannosidase and α-galactosidase) is needed to accomplish their complete hydrolysis. So far, numerous galactomannan-degrading enzymes have been isolated and characterized from extremophilic microorganisms. Besides applications in biorefinery, these biocatalysts are also useful to improve the quality (i.e. digestibility and prebiotic properties) of food and feed as well as in paper industries to aid the pulp bleaching process. In this review, an overview about the structure, function and applications of galactomannans is provided. Moreover, a survey of (hyper)-thermophilic galactomannans-degrading enzymes, mainly characterized in the last decade, has been carried out. These extremozymes are described in the light of their biotechnological application in industrial processes requiring harsh conditions.

Graphical abstract


Thermophiles Galactomannans Galactomannan-degrading enzymes β-mannanase β-mannosidase α-galactosidase 



We thank University of Naples Federico II and Compagnia di San Paolo for the financial support in the frame of the Programme STAR [Grant number, 16-CSP-UNINA-007]. The funding bodies had no influence on the content of the manuscript.


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© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Department of BiologyUniversity of Naples Federico IINaplesItaly

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