Affiliations 

  • 1 Faculty of Bioscience and Medical Engineering, Department of Biotechnology and Medical Engineering, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia; Department of Chemistry/Biochemistry, Federal University Ndufu-Alike Ikwo, PMB, 1010, Ebonyi State, Nigeria; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia
  • 2 School of Chemical and Energy Engineering, Universiti Teknologi Malaysia, 81310, Johor Bahru, Malaysia; Innovation Centre in Agritechnology for Advanced Bioprocessing, UTM Pagoh, Hub Pendidikan Tinggi Pagoh, 84600, Pagoh, Johor. Malaysia
  • 3 Faculty of Bioscience and Medical Engineering, Department of Biotechnology and Medical Engineering, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia
  • 4 Natural Products and Drug Discovery Center, Malaysian Institute of Pharmaceuticals and Nutraceuticals, National Institute of Biotechnology Malaysia, Ministry of Science, Technology and Innovation, Block 5-A, Halaman Bukit Gambir, 11700, Pulau Pinang, Malaysia
  • 5 Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia, 81310, UTM Johor Bahru, Malaysia. Electronic address: roswanira@kimia.fs.utm.my
J Environ Manage, 2019 Aug 01;243:206-217.
PMID: 31096173 DOI: 10.1016/j.jenvman.2019.04.113

Abstract

Production of cellulases and xylanase by a novel Trichoderma asperellum UC1 (GenBank accession no. MF774876) under solid state fermentation (SSF) of raw oil palm frond leaves (OPFL) was optimized. Under optimum fermentation parameters (30 °C, 60-80% moisture content, 2.5 × 106 spores/g inoculum size) maximum CMCase, FPase, β-glucosidase and xylanase activity were recorded at 136.16 IU/g, 26.03 U/g, 130.09 IU/g and 255.01 U/g, respectively. Cellulases and xylanase were produced between a broad pH range of pH 6.0-12.0. The enzyme complex that comprised of four endo-β-1,4-xylanases and endoglucanases, alongside exoglucanase and β-glucosidase showed thermophilic and acidophilic characteristics at 50-60 °C and pH 3.0-4.0, respectively. Glucose (16.87 mg/g) and fructose (18.09 mg/g) were among the dominant sugar products from the in situ hydrolysis of OPFL, aside from cellobiose (105.92 mg/g) and xylose (1.08 mg/g). Thermal and pH stability tests revealed that enzymes CMCase, FPase, β-glucosidase and xylanase retained 50% residual activities for up to 15.18, 4.06, 17.47 and 15.16 h of incubation at 60 °C, as well as 64.59, 25.14, 68.59 and 19.20 h at pH 4.0, respectively. Based on the findings, it appeared that the unique polymeric structure of raw OPFL favored cellulases and xylanase productions.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.