Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL

Abstract

An extracellular xylanase was purified from the mesophilic fungus Penicillium rolfsii c3-2(1) IBRL. After three consecutive purification steps, the extracellular cellulase-free xylanase was successfully purified to homogeneity with a recovery yield of 24%. A single protein band of 35 kDa was detected by SDS-PAGE, which had an optimum catalytic activity at pH 5.0 and 50 °C. This purified enzyme was stable at pH 5 to 7, thermostable up to 55 °C, and retained up to 83% of its activity after 4 hours of pre-incubation. A kinetic study yielded estimated Km and Vmax values of 5.73 mg/mL and 691.6 µmol/min/mg, respectively. Thin layer chromatography experiments showed that the purified xylanase was capable of hydrolyzing xylotriose, xylotetraose, xylopentaose, and xylohexaose but not xylobiose, suggesting it is an endo-xylanase. Enzymatic hydrolysis of oil palm trunk residues by commercial enzymes supplemented with the purified xylanase showed a considerable increase in total sugar conversion compared with the commercial enzymes alone, suggesting that xylanase is a key enzyme in the hydrolysis of oil palm trunk residues.

Biochemical Characteristics of Penicillium crustosum FP 11 Xylanase II and an Assessment of the Properties of Xylanases Produced by the Genus Penicillium

“…The optimal temperature determined for P. crustosum xylanase II was the same obtained for xylanase I of 50°C (Fig. 2A), which was the temperature previously shown to be optimal for P. canescens xylanases [25] and P. rolfsii c3-2(1) IBRL [26]. However, optimal temperatures of 40°C and 80°C have also found for some fungal xylanases of P. occitanis Pol6 [24] and P. funiculosum [27], respectively.…”

Inhibition and kinetic studies of cellulose- and hemicellulose-degrading enzymes ofGanoderma boninenseby naturally occurring phenolic compounds

“…It indicated that the K m and V max values were not only species-specific but also strain specific, hence they can be used as an identification tool. The K m and V max values of xylanase enzymes were more or less equal with xylanase secreted from P. rolfsii (Lee et al 2015). In general, the K m value of the three hydrolytic enzymes of G. boninense is low.…”

“…The K m and V max values of xylanase enzymes were more or less equal with xylanase secreted from P. rolfsii (Lee et al . ). In general, the K m value of the three hydrolytic enzymes of G. boninense is low.…”

Xylanase-producing Fungi Diversity in the Soil of Jeddah, Saudi Arabia

“…They found 30 isolates that produced enzymes that degraded when grown on solid xylan agar. Aspergillus, Trichoderma, and Penicillium are considered rich sources of enzymes for xylan biodegradation [29].…”