Affiliations 

  • 1 Laboratory of Sustainable Animal Production and Biodiversity, Institute of Tropical Agriculture and Food Security, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia. mohdhuzairi@upm.edu.my
  • 2 Department of Biological Function and Engineering, Graduate School of Life Science and System Engineering, Kyushu Institute of Technology, 2-4 Hibikino-cho, Wakamatsu-ku, Fukuoka, 808-0196, Japan
  • 3 Department of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia
  • 4 Advanced Microbiological Functions Research Group, Frontier Research Labs., Institute for Innovation, Ajinomoto, 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki, Japan
Sci Rep, 2019 09 19;9(1):13526.
PMID: 31537863 DOI: 10.1038/s41598-019-50126-y

Abstract

A thermophilic Thermobifida fusca strain UPMC 901, harboring highly thermostable cellulolytic activity, was successfully isolated from oil palm empty fruit bunch compost. Its endoglucanase had the highest activity at 24 hours of incubation in carboxymethyl-cellulose (CMC) and filter paper. A maximum endoglucanase activity of 0.9 U/mL was achieved at pH 5 and 60 °C using CMC as a carbon source. The endoglucanase properties were further characterized using crude enzyme preparations from the culture supernatant. Thermal stability indicated that the endoglucanase activity was highly stable at 70 °C for 24 hours. Furthermore, the activity was found to be completely maintained without any loss at 50 °C and 60 °C for 144 hours, making it the most stable than other endoglucanases reported in the literature. The high stability of the endoglucanase at an elevated temperature for a prolonged period of time makes it a suitable candidate for the biorefinery application.

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