Efficient enzymatic saccharification of macroalgal biomass using a specific thermostable GH 12 endoglucanase from Aspergillus terreus JL1

World J Microbiol Biotechnol. 2019 Dec 12;36(1):5. doi: 10.1007/s11274-019-2779-6.

Abstract

Stranded green macroalgae represents an important and renewable biomass that remains under valorized despite the numerous environmental problems generated by their accumulation in coastal regions. This work describes the isolation of a filamentous thermophile fungus identified as Aspergillus terreus JL1 that produces an efficient cellulolytic activity for green macroalgae saccharification. The characterization of the endoglucanase activity obtained after submerged fermentation showed a differential induction depending on the carbon source used with a unique isoform released when Ulva lactuca was used as inducer. The crude extract obtained hydrolyzed efficiently the untreated algal biomass (70.5%) compared to other cellulolytic extracts. The unique endoglucanase released was then purified to homogeneity (Yield: 49.6%; Specific activity: 30.1 U/mg; Purification fold: 4.36) and characterized biochemically. Its peptidic sequence was then determined and showed its belonging to the GH12. The described enzyme represents a promising biotechnological tool for algal biomass conversion.

Keywords: Alga degradation; Aspergillus terreus JL1; Characterization; Endoglucanase; Purification.

MeSH terms

  • Aspergillus / classification
  • Aspergillus / enzymology*
  • Aspergillus / isolation & purification
  • Biodegradation, Environmental
  • Biomass*
  • Cellulase / isolation & purification
  • Cellulase / metabolism*
  • Cellulose / isolation & purification
  • Cellulose / metabolism
  • DNA, Fungal / isolation & purification
  • Enzyme Stability
  • Fermentation
  • Genomics
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Seaweed / drug effects
  • Seaweed / metabolism*
  • Sequence Analysis
  • Temperature
  • Ulva / drug effects
  • Ulva / metabolism

Substances

  • DNA, Fungal
  • Cellulose
  • Cellulase