Characterization of oil-palm trunk residue degradation enzymes derived from the isolated fungus, Penicillium rolfsii c3-2(1) IBRL

ABSTRACT

This study characterizes crude enzymes derived from Penicillium rolfsii c3-2(1) IBRL, a mesophilic fungus isolated from the local soil of Malaysia. Prior to enzyme activity evaluation, P. rolfsii c3-2(1) IBRL was inoculated into a broth medium containing oil-palm trunk residues for the preparation of crude enzymes. Oil-palm trunk residues were optimally hydrolysed at pH5.0 and 50°C. P. rolfsii c3-2(1) IBRL-derived crude enzymes displayed higher thermal stability compared with the commercial enzymes, Celluclast 1.5 L and Acellerase 1500. Moreover, the hydrolysing activities of the P. rolfsii c3-2(1) IBRL-derived crude enzymes (xylan, arabinan, and laminarin) were superior compared to that of Celluclast 1.5 L and Acellerase 1500, and exhibit 2- to 3-fold and 3- to 4-fold higher oil-palm trunk residues-hydrolysing specific activity, respectively. This higher hydrolysis efficiency may be attributed to the weak ‘lignin-binding’ ability of the P. rolfsii c3-2(1) IBRL-derived enzymes compared to the commercial enzymes.

KEYWORDS:

• Penicillium rolfsii c3-2(1) IBRL
• oil-palm trunk residues
• lignocellulosic biomass
• lignin
• commercial enzymes

Additional information

Funding

We are thankful for the financial support from the Ministry of Higher Education, Malaysia, and for the research grant of Universiti Sains Malaysia-Postgraduate Research Grant Scheme for supporting this project. This work was supported by the Universiti Sains Malaysia [grant number 1001/PBIOLOGI/844098].