A novel detergent-stable protease from Penicillium chrysogenium X5 and its utility in textile fibres processing

Abstract

The consumption of energy and raw-materials, as well as increased awareness of environmental concerns related to the use and disposal of chemicals into landfills, water or release into the air during chemical processing of textiles are the principal reasons for the application of enzymes in finishing of textile materials. The aim of this study is to isolate a new fungi protease, with excellent proprieties in order to be used as a bio-additive in detergent formulation with any destructive effect on textile supports. SAPTEX is a new extracellular thermostable serine alkaline protease (designed as SAPTEX) was purified to homogeneity and biochemically characterized from Penicillium chrysogenium strain X5 as a monomer with 43 kDa. The experimental purification protocol comprises three steps: heat treatment optimized by experimental design followed by an ammonium sulfate precipitation, and a FPLC/UNO Q-12 anion exchange chromatography. The optimum pH and temperature values for protease activity were pH 10 and 80°C, respectively. According to morphological, physico-chemical, and metrological evaluation, SAPTEX has no destructive impact on fibers after the enzyme treatment and a very slight effect on textile support. Data suggested that SAPTEX may be considered a potential candidate as a protein stain removal product from textile supports.