Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola

Jeong Jun Yoon; Chang Jun Cha; Yeong Suk Kim; Wook Kim

doi:10.1007/s10529-008-9715-4

Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola

Jeong Jun Yoon^*
, Chang Jun Cha
, Yeong Suk Kim
, Wook Kim

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

46 Citations (Scopus)

Abstract

An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was ∼32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC. The partial amino acid sequences of the purified endoglucanase had high homology with endo-β-1,4-glucanase of glycosyl hydrolase family 5 from other fungi. The K_m and K_cat values for CMC were 12 mg CMC/ml and 670/s, respectively. The purified EG hydrolyzed both cellotetraose (G4) and cellopentaose (G5), but did not degrade either cellobiose (G2) or cellotriose (G3).

Original language	English
Pages (from-to)	1373-1378
Number of pages	6
Journal	Biotechnology letters
Volume	30
Issue number	8
DOIs	https://doi.org/10.1007/s10529-008-9715-4
Publication status	Published - 2008 Aug

Bibliographical note

Funding Information:
Acknowledgements This study was carried out with the support of Forest Science & Technology Projects (Project No.

Keywords

Brown-rot fungus
Cellulose
Endoglucanase
Fomitopsis pinicola
Microcrystalline cellulose hydrolysis

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-008-9715-4

Cite this

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title = "Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola",

abstract = "An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was ∼32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC. The partial amino acid sequences of the purified endoglucanase had high homology with endo-β-1,4-glucanase of glycosyl hydrolase family 5 from other fungi. The Km and Kcat values for CMC were 12 mg CMC/ml and 670/s, respectively. The purified EG hydrolyzed both cellotetraose (G4) and cellopentaose (G5), but did not degrade either cellobiose (G2) or cellotriose (G3).",

keywords = "Brown-rot fungus, Cellulose, Endoglucanase, Fomitopsis pinicola, Microcrystalline cellulose hydrolysis",

author = "Yoon, \{Jeong Jun\} and Cha, \{Chang Jun\} and Kim, \{Yeong Suk\} and Wook Kim",

note = "Funding Information: Acknowledgements This study was carried out with the support of Forest Science \& Technology Projects (Project No.",

year = "2008",

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doi = "10.1007/s10529-008-9715-4",

language = "English",

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T1 - Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola

AU - Yoon, Jeong Jun

AU - Cha, Chang Jun

AU - Kim, Yeong Suk

AU - Kim, Wook

N1 - Funding Information: Acknowledgements This study was carried out with the support of Forest Science & Technology Projects (Project No.

PY - 2008/8

Y1 - 2008/8

N2 - An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was ∼32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC. The partial amino acid sequences of the purified endoglucanase had high homology with endo-β-1,4-glucanase of glycosyl hydrolase family 5 from other fungi. The Km and Kcat values for CMC were 12 mg CMC/ml and 670/s, respectively. The purified EG hydrolyzed both cellotetraose (G4) and cellopentaose (G5), but did not degrade either cellobiose (G2) or cellotriose (G3).

AB - An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was ∼32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC. The partial amino acid sequences of the purified endoglucanase had high homology with endo-β-1,4-glucanase of glycosyl hydrolase family 5 from other fungi. The Km and Kcat values for CMC were 12 mg CMC/ml and 670/s, respectively. The purified EG hydrolyzed both cellotetraose (G4) and cellopentaose (G5), but did not degrade either cellobiose (G2) or cellotriose (G3).

KW - Brown-rot fungus

KW - Cellulose

KW - Endoglucanase

KW - Fomitopsis pinicola

KW - Microcrystalline cellulose hydrolysis

UR - https://www.scopus.com/pages/publications/45849139328

U2 - 10.1007/s10529-008-9715-4

DO - 10.1007/s10529-008-9715-4

M3 - Article

C2 - 18414798

AN - SCOPUS:45849139328

SN - 0141-5492

VL - 30

SP - 1373

EP - 1378

JO - Biotechnology letters

JF - Biotechnology letters

IS - 8

ER -

Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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