Characterization of a β-1,4-mannanase from a newly isolated strain of Pholiota adiposa and its application for biomass pretreatment

Priyadharshini Ramachandran; Zongpei Zhao; Raushan Singh; Saurabh Sudha Dhiman; Joon Ho Choi; Dongwook Kim; Jung Rim Haw; Jung Kul Lee

doi:10.1007/s00449-014-1156-y

Characterization of a β-1,4-mannanase from a newly isolated strain of Pholiota adiposa and its application for biomass pretreatment

Priyadharshini Ramachandran, Zongpei Zhao, Raushan Singh, Saurabh Sudha Dhiman, Joon Ho Choi, Dongwook Kim, Jung Rim Haw^*, Jung Kul Lee

^*Corresponding author for this work

Department of Chemistry

7 Citations (Scopus)

Abstract

A highly efficient β-1,4-mannanase-secreting strain, Pholiota adiposa SKU0714, was isolated and identified on the basis of its morphological features and sequence analysis of internal transcribed spacer rDNA. P. adiposa β-1,4-mannanase was purified to homogeneity from P. adiposa culture supernatants by one-step chromatography on a Sephacryl gel filtration column. P. adiposa β-1,4-mannanase showed the highest activity toward locust bean gum (V _max = 1,990 U/mg protein, K _m = 0.12 mg/mL) ever reported. Its internal amino acid sequence showed homology with hydrolases from the glycoside hydrolase family 5 (GH5), indicating that the enzyme is a member of the GH5 family. The saccharification of commercial mannanase and P. adiposa β-1,4-mannanase-pretreated rice straw by Celluclast 1.5L (Novozymes) was compared. In comparison with the commercial Novo Mannaway^® (113 mg/g-substrate), P. adiposa β-1,4-mannanase-pretreated rice straw released more reducing sugars (141 mg/g-substrate). These properties make P. adiposa β-1,4-mannanase a good candidate as a new commercial β-1,4-mannanase to improve biomass pretreatment.

Original language	English
Journal	Bioprocess and Biosystems Engineering
Volume	37
Issue number	9
Pages (from-to)	1817-1824
Number of pages	8
ISSN	1615-7591
DOIs	https://doi.org/10.1007/s00449-014-1156-y
Publication status	Published - Sept 2014

Keywords

Enzyme purification
Glycoside hydrolase
Manganese ion dependent
Pholiota adiposa
β-1,4-Mannanase

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10.1007/s00449-014-1156-y

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Characterization of a β-1,4-mannanase from a newly isolated strain of Pholiota adiposa and its application for biomass pretreatment. / Ramachandran, Priyadharshini; Zhao, Zongpei; Singh, Raushan et al.

In: Bioprocess and Biosystems Engineering, Vol. 37, No. 9, 09.2014, p. 1817-1824.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "A highly efficient β-1,4-mannanase-secreting strain, Pholiota adiposa SKU0714, was isolated and identified on the basis of its morphological features and sequence analysis of internal transcribed spacer rDNA. P. adiposa β-1,4-mannanase was purified to homogeneity from P. adiposa culture supernatants by one-step chromatography on a Sephacryl gel filtration column. P. adiposa β-1,4-mannanase showed the highest activity toward locust bean gum (V max = 1,990 U/mg protein, K m = 0.12 mg/mL) ever reported. Its internal amino acid sequence showed homology with hydrolases from the glycoside hydrolase family 5 (GH5), indicating that the enzyme is a member of the GH5 family. The saccharification of commercial mannanase and P. adiposa β-1,4-mannanase-pretreated rice straw by Celluclast 1.5L (Novozymes) was compared. In comparison with the commercial Novo Mannaway{\textregistered} (113 mg/g-substrate), P. adiposa β-1,4-mannanase-pretreated rice straw released more reducing sugars (141 mg/g-substrate). These properties make P. adiposa β-1,4-mannanase a good candidate as a new commercial β-1,4-mannanase to improve biomass pretreatment.",

keywords = "Enzyme purification, Glycoside hydrolase, Manganese ion dependent, Pholiota adiposa, β-1,4-Mannanase",

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AU - Zhao, Zongpei

AU - Singh, Raushan

AU - Dhiman, Saurabh Sudha

AU - Choi, Joon Ho

AU - Kim, Dongwook

AU - Haw, Jung Rim

AU - Lee, Jung Kul

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AB - A highly efficient β-1,4-mannanase-secreting strain, Pholiota adiposa SKU0714, was isolated and identified on the basis of its morphological features and sequence analysis of internal transcribed spacer rDNA. P. adiposa β-1,4-mannanase was purified to homogeneity from P. adiposa culture supernatants by one-step chromatography on a Sephacryl gel filtration column. P. adiposa β-1,4-mannanase showed the highest activity toward locust bean gum (V max = 1,990 U/mg protein, K m = 0.12 mg/mL) ever reported. Its internal amino acid sequence showed homology with hydrolases from the glycoside hydrolase family 5 (GH5), indicating that the enzyme is a member of the GH5 family. The saccharification of commercial mannanase and P. adiposa β-1,4-mannanase-pretreated rice straw by Celluclast 1.5L (Novozymes) was compared. In comparison with the commercial Novo Mannaway® (113 mg/g-substrate), P. adiposa β-1,4-mannanase-pretreated rice straw released more reducing sugars (141 mg/g-substrate). These properties make P. adiposa β-1,4-mannanase a good candidate as a new commercial β-1,4-mannanase to improve biomass pretreatment.

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Characterization of a β-1,4-mannanase from a newly isolated strain of Pholiota adiposa and its application for biomass pretreatment

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