Enantioselective production of levofloxacin by immobilized porcine liver esterase

Sang Yoon Lee; Byung Hyuk Min; Sung Ho Hwang; Yoon Mo Koo; Choul Kyun Lee; Seong Won Song; Sun Young Oh; Sang Min Lim; Sang Lin Kim; Dong II Kim

doi:10.1023/A:1010554118301

Enantioselective production of levofloxacin by immobilized porcine liver esterase

Sang Yoon Lee, Byung Hyuk Min, Sung Ho Hwang, Yoon Mo Koo, Choul Kyun Lee, Seong Won Song, Sun Young Oh, Sang Min Lim, Sang Lin Kim, Dong II Kim

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

16 Scopus citations

Abstract

Porcine liver esterase, which cleaves ofloxacin butyl ester enantioselectively to levofloxacin, was successfully immobilized in calcium alginate and polyacrylamide gel. Immobilized esterase in 5% (w/v) calcium alginate exhibited 58% immobilization efficiency and could be reused five times without severe loss of enzyme activity. On the other hand, entrapped esterase in polyacrylamide gel, composed of 20% of total monomer and 8.3% of cross-linking agent, could be reused 10 times, and 51% of enzyme activity remained after the 10th batch without decrease of enantioselectivity. Compared with entrapped methods, significant reduction of enzyme activity was found in the case of physical adsorption on to QAE-Sephadex.

Original language	English
Pages (from-to)	1033-1037
Number of pages	5
Journal	Biotechnology Letters
Volume	23
Issue number	13
DOIs	https://doi.org/10.1023/A:1010554118301
State	Published - 2001

Bibliographical note

Funding Information:
This work was supported by the Center of Advanced Bioseparation Technology, Inha University. The support is deeply appreciated.

Keywords

Immobilized enzyme
Levofloxacin
Ofloxacin
Porcine liver esterase

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10.1023/A:1010554118301

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@article{619db10b4ded4257a270cb3768b3623e,

title = "Enantioselective production of levofloxacin by immobilized porcine liver esterase",

abstract = "Porcine liver esterase, which cleaves ofloxacin butyl ester enantioselectively to levofloxacin, was successfully immobilized in calcium alginate and polyacrylamide gel. Immobilized esterase in 5% (w/v) calcium alginate exhibited 58% immobilization efficiency and could be reused five times without severe loss of enzyme activity. On the other hand, entrapped esterase in polyacrylamide gel, composed of 20% of total monomer and 8.3% of cross-linking agent, could be reused 10 times, and 51% of enzyme activity remained after the 10th batch without decrease of enantioselectivity. Compared with entrapped methods, significant reduction of enzyme activity was found in the case of physical adsorption on to QAE-Sephadex.",

keywords = "Immobilized enzyme, Levofloxacin, Ofloxacin, Porcine liver esterase",

author = "Lee, {Sang Yoon} and Min, {Byung Hyuk} and Hwang, {Sung Ho} and Koo, {Yoon Mo} and Lee, {Choul Kyun} and Song, {Seong Won} and Oh, {Sun Young} and Lim, {Sang Min} and Kim, {Sang Lin} and Kim, {Dong II}",

note = "Funding Information: This work was supported by the Center of Advanced Bioseparation Technology, Inha University. The support is deeply appreciated.",

year = "2001",

doi = "10.1023/A:1010554118301",

language = "English",

volume = "23",

pages = "1033--1037",

journal = "Biotechnology Letters",

issn = "0141-5492",

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

number = "13",

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TY - JOUR

T1 - Enantioselective production of levofloxacin by immobilized porcine liver esterase

AU - Lee, Sang Yoon

AU - Min, Byung Hyuk

AU - Hwang, Sung Ho

AU - Koo, Yoon Mo

AU - Lee, Choul Kyun

AU - Song, Seong Won

AU - Oh, Sun Young

AU - Lim, Sang Min

AU - Kim, Sang Lin

AU - Kim, Dong II

N1 - Funding Information: This work was supported by the Center of Advanced Bioseparation Technology, Inha University. The support is deeply appreciated.

PY - 2001

Y1 - 2001

N2 - Porcine liver esterase, which cleaves ofloxacin butyl ester enantioselectively to levofloxacin, was successfully immobilized in calcium alginate and polyacrylamide gel. Immobilized esterase in 5% (w/v) calcium alginate exhibited 58% immobilization efficiency and could be reused five times without severe loss of enzyme activity. On the other hand, entrapped esterase in polyacrylamide gel, composed of 20% of total monomer and 8.3% of cross-linking agent, could be reused 10 times, and 51% of enzyme activity remained after the 10th batch without decrease of enantioselectivity. Compared with entrapped methods, significant reduction of enzyme activity was found in the case of physical adsorption on to QAE-Sephadex.

AB - Porcine liver esterase, which cleaves ofloxacin butyl ester enantioselectively to levofloxacin, was successfully immobilized in calcium alginate and polyacrylamide gel. Immobilized esterase in 5% (w/v) calcium alginate exhibited 58% immobilization efficiency and could be reused five times without severe loss of enzyme activity. On the other hand, entrapped esterase in polyacrylamide gel, composed of 20% of total monomer and 8.3% of cross-linking agent, could be reused 10 times, and 51% of enzyme activity remained after the 10th batch without decrease of enantioselectivity. Compared with entrapped methods, significant reduction of enzyme activity was found in the case of physical adsorption on to QAE-Sephadex.

KW - Immobilized enzyme

KW - Levofloxacin

KW - Ofloxacin

KW - Porcine liver esterase

UR - http://www.scopus.com/inward/record.url?scp=0034902686&partnerID=8YFLogxK

U2 - 10.1023/A:1010554118301

DO - 10.1023/A:1010554118301

M3 - Article

AN - SCOPUS:0034902686

SN - 0141-5492

VL - 23

SP - 1033

EP - 1037

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 13

ER -

Enantioselective production of levofloxacin by immobilized porcine liver esterase

Abstract

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