Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles

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Standard

Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles. / Singh, Raushan Kumar; Zhang, Ye Wang; Nguyen, Ngoc Phuong Thao; Jeya, Marimuthu; Lee, Jung Kul.

I: Applied Microbiology and Biotechnology, Bind 89, Nr. 2, 01.01.2011, s. 337-344.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Singh, RK, Zhang, YW, Nguyen, NPT, Jeya, M & Lee, JK 2011, 'Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles', Applied Microbiology and Biotechnology, bind 89, nr. 2, s. 337-344. https://doi.org/10.1007/s00253-010-2768-z

APA

Singh, R. K., Zhang, Y. W., Nguyen, N. P. T., Jeya, M., & Lee, J. K. (2011). Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles. Applied Microbiology and Biotechnology, 89(2), 337-344. https://doi.org/10.1007/s00253-010-2768-z

Vancouver

Singh RK, Zhang YW, Nguyen NPT, Jeya M, Lee JK. Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles. Applied Microbiology and Biotechnology. 2011 jan 1;89(2):337-344. https://doi.org/10.1007/s00253-010-2768-z

Author

Singh, Raushan Kumar ; Zhang, Ye Wang ; Nguyen, Ngoc Phuong Thao ; Jeya, Marimuthu ; Lee, Jung Kul. / Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles. I: Applied Microbiology and Biotechnology. 2011 ; Bind 89, Nr. 2. s. 337-344.

Bibtex

@article{91a8ed249c614f3eb5192e4cfd960af9,
title = "Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles",
abstract = "An efficient β-1,4-glucosidase (BGL) secreting strain, Agaricus arvensis, was isolated and identified. The relative molecular weight of the purified A. arvensis BGL was 98 kDa, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis, or 780 kDa by size exclusion chromatography, indicating that the enzyme is an octamer. Using a crude enzyme preparation, A. arvensis BGL was covalently immobilized onto functionalized silicon oxide nanoparticles with an immobilization efficiency of 158%. The apparent V max (k cat) values of free and immobilized BGL under standard assay conditions were 3,028 U mg protein-1 (4,945 s -1) and 3,347 U mg protein-1 (5,466 s-1), respectively. The immobilized BGL showed a higher optimum temperature and improved thermostability as compared to the free enzyme. The half-life at 65 °C showed a 288-fold improvement over the free BGL. After 25 cycles, the immobilized enzyme still retained 95% of the original activity, thus demonstrating its prospects for commercial applications. High specific activity, high immobilization efficiency, improved stability, and reusability of A. arvensis BGL make this enzyme of potential interest in a number of industrial applications.",
keywords = "β-1-4-Glucosidase, Covalent bonding, Immobilization, Silicon oxide nanoparticles",
author = "Singh, {Raushan Kumar} and Zhang, {Ye Wang} and Nguyen, {Ngoc Phuong Thao} and Marimuthu Jeya and Lee, {Jung Kul}",
year = "2011",
month = jan,
day = "1",
doi = "10.1007/s00253-010-2768-z",
language = "English",
volume = "89",
pages = "337--344",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer",
number = "2",

}

RIS

TY - JOUR

T1 - Covalent immobilization of β-1,4-glucosidase from Agaricus arvensis onto functionalized silicon oxide nanoparticles

AU - Singh, Raushan Kumar

AU - Zhang, Ye Wang

AU - Nguyen, Ngoc Phuong Thao

AU - Jeya, Marimuthu

AU - Lee, Jung Kul

PY - 2011/1/1

Y1 - 2011/1/1

N2 - An efficient β-1,4-glucosidase (BGL) secreting strain, Agaricus arvensis, was isolated and identified. The relative molecular weight of the purified A. arvensis BGL was 98 kDa, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis, or 780 kDa by size exclusion chromatography, indicating that the enzyme is an octamer. Using a crude enzyme preparation, A. arvensis BGL was covalently immobilized onto functionalized silicon oxide nanoparticles with an immobilization efficiency of 158%. The apparent V max (k cat) values of free and immobilized BGL under standard assay conditions were 3,028 U mg protein-1 (4,945 s -1) and 3,347 U mg protein-1 (5,466 s-1), respectively. The immobilized BGL showed a higher optimum temperature and improved thermostability as compared to the free enzyme. The half-life at 65 °C showed a 288-fold improvement over the free BGL. After 25 cycles, the immobilized enzyme still retained 95% of the original activity, thus demonstrating its prospects for commercial applications. High specific activity, high immobilization efficiency, improved stability, and reusability of A. arvensis BGL make this enzyme of potential interest in a number of industrial applications.

AB - An efficient β-1,4-glucosidase (BGL) secreting strain, Agaricus arvensis, was isolated and identified. The relative molecular weight of the purified A. arvensis BGL was 98 kDa, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis, or 780 kDa by size exclusion chromatography, indicating that the enzyme is an octamer. Using a crude enzyme preparation, A. arvensis BGL was covalently immobilized onto functionalized silicon oxide nanoparticles with an immobilization efficiency of 158%. The apparent V max (k cat) values of free and immobilized BGL under standard assay conditions were 3,028 U mg protein-1 (4,945 s -1) and 3,347 U mg protein-1 (5,466 s-1), respectively. The immobilized BGL showed a higher optimum temperature and improved thermostability as compared to the free enzyme. The half-life at 65 °C showed a 288-fold improvement over the free BGL. After 25 cycles, the immobilized enzyme still retained 95% of the original activity, thus demonstrating its prospects for commercial applications. High specific activity, high immobilization efficiency, improved stability, and reusability of A. arvensis BGL make this enzyme of potential interest in a number of industrial applications.

KW - β-1-4-Glucosidase

KW - Covalent bonding

KW - Immobilization

KW - Silicon oxide nanoparticles

UR - http://www.scopus.com/inward/record.url?scp=78651086201&partnerID=8YFLogxK

U2 - 10.1007/s00253-010-2768-z

DO - 10.1007/s00253-010-2768-z

M3 - Journal article

C2 - 20811797

AN - SCOPUS:78651086201

VL - 89

SP - 337

EP - 344

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 2

ER -

ID: 229901266