Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO2 whiskers

H. Q. Wang; Zhong Yao; Y. Sun; Z. Zhou; Q. Xiong; Z. X. Zhong

doi:10.1007/s12257-013-0675-8

Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO₂ whiskers

H. Q. Wang, Zhong Yao, Y. Sun, Z. Zhou, Q. Xiong, Z. X. Zhong

Nanjing Tech University

科研成果: 期刊稿件 › 文章 › 同行评审

22 引用（Scopus）

摘要

The surface of mesoporous TiO₂ whiskers (MTw) was chemically modified with 3-aminopropyltriethoxysilane (APTES). The point of zero charge (pzc) of MTw and the modified material (MTwA) was 5.3 and 6.8, respectively. MTw and MTwA were then used as carrier to immobilize γ-glutamyltranspeptidase (GGT) from Bacillus subtilis (B. subtilis). Our results indicated that the loading capacity of MTwA for GTT was significantly superior to that of MTw. Although the optimum temperature and thermal stability of MTwA-GGT were slightly lower than those of MTw-GGT, its pH stability was greatly improved compared with either free enzyme or MTw-GGT. The affinity constant (K_m) of MTwA-GGT to γ-glutamyl-p-nitroanilide (GpNA) was 0.889 mM, higher than that of free enzyme but lower than that of MTw-GGT. In addition, MTwA-GGT displayed a good operational stability.

源语言	英语
页（从-至）	304-310
页数	7
期刊	Biotechnology and Bioprocess Engineering
卷	19
期	2
DOI	https://doi.org/10.1007/s12257-013-0675-8
出版状态	已出版 - 3月 2014

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title = "Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO2 whiskers",

abstract = "The surface of mesoporous TiO2 whiskers (MTw) was chemically modified with 3-aminopropyltriethoxysilane (APTES). The point of zero charge (pzc) of MTw and the modified material (MTwA) was 5.3 and 6.8, respectively. MTw and MTwA were then used as carrier to immobilize γ-glutamyltranspeptidase (GGT) from Bacillus subtilis (B. subtilis). Our results indicated that the loading capacity of MTwA for GTT was significantly superior to that of MTw. Although the optimum temperature and thermal stability of MTwA-GGT were slightly lower than those of MTw-GGT, its pH stability was greatly improved compared with either free enzyme or MTw-GGT. The affinity constant (Km) of MTwA-GGT to γ-glutamyl-p-nitroanilide (GpNA) was 0.889 mM, higher than that of free enzyme but lower than that of MTw-GGT. In addition, MTwA-GGT displayed a good operational stability.",

keywords = "3-aminopropyltriethyloxysilane, chemical modification, immobilization, stability, γ-glutamyltranspeptidase",

author = "Wang, {H. Q.} and Zhong Yao and Y. Sun and Z. Zhou and Q. Xiong and Zhong, {Z. X.}",

year = "2014",

month = mar,

doi = "10.1007/s12257-013-0675-8",

language = "英语",

volume = "19",

pages = "304--310",

journal = "Biotechnology and Bioprocess Engineering",

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TY - JOUR

T1 - Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO2 whiskers

AU - Wang, H. Q.

AU - Yao, Zhong

AU - Sun, Y.

AU - Zhou, Z.

AU - Xiong, Q.

AU - Zhong, Z. X.

PY - 2014/3

Y1 - 2014/3

N2 - The surface of mesoporous TiO2 whiskers (MTw) was chemically modified with 3-aminopropyltriethoxysilane (APTES). The point of zero charge (pzc) of MTw and the modified material (MTwA) was 5.3 and 6.8, respectively. MTw and MTwA were then used as carrier to immobilize γ-glutamyltranspeptidase (GGT) from Bacillus subtilis (B. subtilis). Our results indicated that the loading capacity of MTwA for GTT was significantly superior to that of MTw. Although the optimum temperature and thermal stability of MTwA-GGT were slightly lower than those of MTw-GGT, its pH stability was greatly improved compared with either free enzyme or MTw-GGT. The affinity constant (Km) of MTwA-GGT to γ-glutamyl-p-nitroanilide (GpNA) was 0.889 mM, higher than that of free enzyme but lower than that of MTw-GGT. In addition, MTwA-GGT displayed a good operational stability.

AB - The surface of mesoporous TiO2 whiskers (MTw) was chemically modified with 3-aminopropyltriethoxysilane (APTES). The point of zero charge (pzc) of MTw and the modified material (MTwA) was 5.3 and 6.8, respectively. MTw and MTwA were then used as carrier to immobilize γ-glutamyltranspeptidase (GGT) from Bacillus subtilis (B. subtilis). Our results indicated that the loading capacity of MTwA for GTT was significantly superior to that of MTw. Although the optimum temperature and thermal stability of MTwA-GGT were slightly lower than those of MTw-GGT, its pH stability was greatly improved compared with either free enzyme or MTw-GGT. The affinity constant (Km) of MTwA-GGT to γ-glutamyl-p-nitroanilide (GpNA) was 0.889 mM, higher than that of free enzyme but lower than that of MTw-GGT. In addition, MTwA-GGT displayed a good operational stability.

KW - 3-aminopropyltriethyloxysilane

KW - chemical modification

KW - immobilization

KW - stability

KW - γ-glutamyltranspeptidase

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U2 - 10.1007/s12257-013-0675-8

DO - 10.1007/s12257-013-0675-8

M3 - 文章

AN - SCOPUS:84901199100

SN - 1226-8372

VL - 19

SP - 304

EP - 310

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

IS - 2

ER -

Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO2 whiskers

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Immobilization of γ-glutamyltranspeptidase on silylated mesoporous TiO₂ whiskers