Laundry Detergent Compatibility and Dehairing Efficiency of Alkaline Thermostable Protease Produced from Aspergillus terreus under Solid-state Fermentation

J Oleo Sci. 2020;69(3):241-254. doi: 10.5650/jos.ess19315.

Abstract

Aspergillus terreus was chosen for production of alkaline protease using solid-state fermentation (SSF). The maximum enzyme yield reached about 34.87 U/mg protein after optimization of fermentation parameters. The produced alkaline protease was purified by precipitation with iso-propanol and then purified through gel filtration and ion exchange column chromatography with a yield of 53.58% and 5.09- fold purification. The enzyme has shown to have a molecular weight of 35 kDa. Optimal pH and temperature for the enzyme activity were 9.5 and 50°C respectively. The highest activity was reported towards casein, with an apparent Km value of 6.66 mg/mL and Vmax was 30 U/mL. The enzyme activity was greatly repressed by phenylmethylsulfonyl fluoride (PMSF). Sodium dodecyl sulfate (SDS) caused activation in enzyme activity. The enzyme retained about 83.8, 70.6, 74.5, 76.4 and 66.4% of its original activity after incubation with Aerial, Leader, Oxi, Persil and Tide, respectively for 8 h at 60°C. Adding of the enzyme in detergents improved the cleansing performance to the blood stains and suggested to be used as a detergent additive. Our outcomes showed that protease could be used as environment green-approach in dehairing process.

Keywords: Aspergillus terreus; alkaline protease; dehairing efficiency; detergent compatibility; purification; wheat straw.

MeSH terms

  • Aspergillus / metabolism*
  • Detergents*
  • Enzyme Activation / drug effects
  • Fermentation*
  • Hydrogen-Ion Concentration
  • Phenylmethylsulfonyl Fluoride / pharmacology
  • Serine Endopeptidases* / isolation & purification
  • Serine Endopeptidases* / metabolism
  • Sodium Dodecyl Sulfate / pharmacology
  • Temperature

Substances

  • Detergents
  • Sodium Dodecyl Sulfate
  • Phenylmethylsulfonyl Fluoride
  • Serine Endopeptidases
  • oryzin