• Journal of the Korean Wood Science and Technology
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• 제47권6호
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• pp.751-760
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• 2019

Cellulase is an eco-friendly biocatalyst, and its demand is growing in many industrial applications such as food, textile, paper, and bioenergy. Strains with a high cellulase activities are the starting point for the economic production of cellulase. In a previous study, Acanthophysium sp. KMF001 with high cellulase production ability was selected among 54 wood-rotting fungi. In this study, we evaluated the cellulase productivity of Acanthophysium sp. KMF001 quantitatively and analyzed its taxonomic location using a genetic method. Acanthophysium sp. KMF001 showed high cellulase productivity similar to that of Acanthophysium bisporum and was much better than A. bisporum in specific enzyme activity. The 28S rRNA sequence of Acanthophysium sp. KMF001 was similar to that of Acanthophysium lividocaeruleum MB1825, with 98.40% homology. Phylogenetic analysis suggested that Acanthophysium sp. KMF001 is a new strain. In this study, we propose a new strain with high cellulase productivity.

• Journal of the Korean Wood Science and Technology
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• 제44권3호
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• pp.381-388
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• 2016

면직물 표면의 잔털을 제거하여 새 옷 같은 느낌을 주기 위한 환경친화적 방법으로 셀룰라아제를 이용한 바이오폴리싱 방법이 도입되어 산업적으로 널리 이용되고 있다. 본 연구에서는 목재의 당화능력이 우수한 Acanthophysium sp. KMF001 효소를 분리해내어 이 효소의 바이오폴리싱 효과를 평가하였다. 실험을 통해 선정한 최적 바이오폴리싱 처리조건은 $50^{\circ}C$, pH 4.5, 처리효소농도는 면직물 중량 대비 10%, 반응시간은 60분으로 나타났다. 실험결과 최적화된 조건에서 처리한 면직물의 인장강도는 감소율이 상업용 효소보다 적었으며 전자현미경 관찰결과 잔털제거효과가 우수하여 바이오폴리싱 효과가 있는 것으로 평가되었다. 따라서 실험에 사용한 Acanthophysium sp. KMF001이 바이오폴리싱에 효과적으로 적용 가능한 효소로 판단된다.

• Journal of the Korean Wood Science and Technology
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• 제46권6호
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• pp.670-680
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• 2018

Acanthophysium sp. KMF001, a wood rotting fungus, produces a strong crude enzyme complex that efficiently produces simple sugars from wood. The transcriptomic analysis of Acanthophysium sp. KMF001 identified 14 genes for putative glycoside hydrolases. Among them, isotig01043 was expressed heterogeneously in Escherichia coli BL21(DE3), and the expressed protein exhibited an endo-${\beta}$-1,4-xylanase activity which showed the optimum reaction at pH 5.0 and $30^{\circ}C$. The enzyme kinetic values of $K_m$ and $V_{max}$ were 25.92 mg/ml and $0.628{\mu}mole/mg/ml$, respectively. The enzymatic characteristics of the expressed xylanase showed a typical fungal xylanase. However, the bioinformatics analysis suggested that the protein encoded by isotig01043 was a novel xylanase based on a low identity when it was compared with the closest protein in the NCBI database and a similar protein domain with GH16_fungal_Lam16A_glucanase, which had not been earlier suggested as a xylanase.