Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium

Nguyen Duc Huy; Palvannan Thayumanavan; Tae Ho Kwon; Seung Moon Park

doi:10.1016/j.jbiosc.2013.02.004

Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium

Nguyen Duc Huy
, Palvannan Thayumanavan
, Tae Ho Kwon
, Seung Moon Park^*

^*Corresponding author for this work

Department of Bioenvironmental Chemistry

Jeonbuk National University
Hue University
Periyar University
Natural Bio-Materials Inc.

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

43 Scopus citations

Abstract

A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141Ul^-1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83kDa. Cu²⁺ and Zn²⁺ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.

Original language	English
Pages (from-to)	152-159
Number of pages	8
Journal	Journal of Bioscience and Bioengineering
Volume	116
Issue number	2
DOIs	https://doi.org/10.1016/j.jbiosc.2013.02.004
State	Published - 2013.08

Keywords

Arabinofuranosidase
Phanerochaete chrysosporium
Pichia pastoris
Xylan
Xylose
Xylosidase

Quacquarelli Symonds(QS) Subject Topics

Engineering - Chemical
Biological Sciences

Access to Document

10.1016/j.jbiosc.2013.02.004

Cite this

@article{9671e9d360f742808406eaccd28bd75e,

title = "Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium",

abstract = "A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141Ul-1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83kDa. Cu2+ and Zn2+ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151\%, 126\% and 123\%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.",

keywords = "Arabinofuranosidase, Phanerochaete chrysosporium, Pichia pastoris, Xylan, Xylose, Xylosidase",

author = "Huy, \{Nguyen Duc\} and Palvannan Thayumanavan and Kwon, \{Tae Ho\} and Park, \{Seung Moon\}",

year = "2013",

month = aug,

doi = "10.1016/j.jbiosc.2013.02.004",

language = "English",

volume = "116",

pages = "152--159",

journal = "Journal of Bioscience and Bioengineering",

issn = "1389-1723",

number = "2",

}

TY - JOUR

T1 - Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium

AU - Huy, Nguyen Duc

AU - Thayumanavan, Palvannan

AU - Kwon, Tae Ho

AU - Park, Seung Moon

PY - 2013/8

Y1 - 2013/8

N2 - A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141Ul-1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83kDa. Cu2+ and Zn2+ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.

AB - A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141Ul-1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83kDa. Cu2+ and Zn2+ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC.

KW - Arabinofuranosidase

KW - Phanerochaete chrysosporium

KW - Pichia pastoris

KW - Xylan

KW - Xylose

KW - Xylosidase

UR - https://www.scopus.com/pages/publications/84879099738

U2 - 10.1016/j.jbiosc.2013.02.004

DO - 10.1016/j.jbiosc.2013.02.004

M3 - Journal article

C2 - 23474097

AN - SCOPUS:84879099738

SN - 1389-1723

VL - 116

SP - 152

EP - 159

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

IS - 2

ER -

Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium

Abstract

Keywords

Quacquarelli Symonds(QS) Subject Topics

Access to Document

Other files and links

Fingerprint

Cite this