Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

Sangpill Hwang; Jungoh Ahn; Sumin Lee; Tai Gyu Lee; Seungjoo Haam; Kangtaek Lee; Ik Sung Ahn; Joon Ki Jung

doi:10.1023/B:BILE.0000021964.69500.6f

Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

Sangpill Hwang, Jungoh Ahn, Sumin Lee, Tai Gyu Lee, Seungjoo Haam, Kangtaek Lee, Ik Sung Ahn, Joon Ki Jung

Department of Chemical and Biomolecular Engineering

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

35 Citations (Scopus)

Abstract

A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

Original language	English
Pages (from-to)	603-605
Number of pages	3
Journal	Biotechnology Letters
Volume	26
Issue number	7
DOIs	https://doi.org/10.1023/B:BILE.0000021964.69500.6f
Publication status	Published - 2004 Apr

Bibliographical note

Funding Information:
This work was made possible with funding provided by the Korea Science & Engineering Foundation to Advanced Environmental Biotechnology Research Center at POSTECH.

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1023/B:BILE.0000021964.69500.6f

Cite this

@article{46e7131d77dc4d3abcb160faecd8456f,

title = "Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization",

abstract = "A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.",

keywords = "Adsorption, Avicel, Cellulose-binding domain, Immobilization, Lipase",

author = "Sangpill Hwang and Jungoh Ahn and Sumin Lee and Lee, {Tai Gyu} and Seungjoo Haam and Kangtaek Lee and Ahn, {Ik Sung} and Jung, {Joon Ki}",

note = "Funding Information: This work was made possible with funding provided by the Korea Science & Engineering Foundation to Advanced Environmental Biotechnology Research Center at POSTECH.",

year = "2004",

month = apr,

doi = "10.1023/B:BILE.0000021964.69500.6f",

language = "English",

volume = "26",

pages = "603--605",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

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TY - JOUR

T1 - Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

AU - Hwang, Sangpill

AU - Ahn, Jungoh

AU - Lee, Sumin

AU - Lee, Tai Gyu

AU - Haam, Seungjoo

AU - Lee, Kangtaek

AU - Ahn, Ik Sung

AU - Jung, Joon Ki

N1 - Funding Information: This work was made possible with funding provided by the Korea Science & Engineering Foundation to Advanced Environmental Biotechnology Research Center at POSTECH.

PY - 2004/4

Y1 - 2004/4

N2 - A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

AB - A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

KW - Adsorption

KW - Avicel

KW - Cellulose-binding domain

KW - Immobilization

KW - Lipase

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U2 - 10.1023/B:BILE.0000021964.69500.6f

DO - 10.1023/B:BILE.0000021964.69500.6f

M3 - Article

C2 - 15168862

AN - SCOPUS:1842760467

SN - 0141-5492

VL - 26

SP - 603

EP - 605

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 7

ER -

Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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