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

TY - JOUR

T1 - Characterization of a β-1,4-mannanase from a newly isolated strain of Pholiota adiposa and its application for biomass pretreatment

AU - Ramachandran, Priyadharshini

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

PY - 2014/9

Y1 - 2014/9

N2 - 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.

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.

KW - Enzyme purification

KW - Glycoside hydrolase

KW - Manganese ion dependent

KW - Pholiota adiposa

KW - β-1,4-Mannanase

UR - http://www.scopus.com/inward/record.url?scp=84906947855&partnerID=8YFLogxK

U2 - 10.1007/s00449-014-1156-y

DO - 10.1007/s00449-014-1156-y

M3 - Journal article

C2 - 24590240

AN - SCOPUS:84906947855

SN - 1615-7591

VL - 37

SP - 1817

EP - 1824

JO - Bioprocess and Biosystems Engineering

JF - Bioprocess and Biosystems Engineering

IS - 9

ER -