Modification of lipase from Candida rugosa with poly(ethylene oxide-co-maleic anhydride) and its separation using aqueous two-phase partition system

Kwinam Park, Seungmoon Lee, Sanjeev Maken, Wongun Koh, Byoungryul Min, Jinwon Park

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A copolymer was synthesized from polyethylene oxide (PEO) and maleic acid anhydride (MA). Number of ethylene oxide units was varied from 10 to 40. Lipase from Candida nigosa was modified through chemical bonding of MA with amino group of lipase. Degree of modification increased with a decrease in EO unit and increase in copolymer/enzyme ratio. The relative activity of modified enzyme increased with increase in EO unit. It was more than native lipase (100%) when copolymer/enzyme weight ratio was less than 3 for all copolymers. It might be due the conformation change of the lipase molecules on modification that would have exposed the catalytic sites making them more easily accessible. At the highest DM (39%), modified lipase retained more than 50% relative activity. Partitioning of native and modified lipase was also studied by using aqueous two phase synthesized copolymer/dextran system: modified lipase (with EO 30 and 40) showed better separation than the native one. Partition coefficient increased with increase in copolymer/enzyme weight ratio.

Original languageEnglish
Pages (from-to)601-606
Number of pages6
JournalKorean Journal of Chemical Engineering
Volume23
Issue number4
DOIs
Publication statusPublished - 2006 Jul 1

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Maleic Anhydrides
Candida
Lipases
Maleic anhydride
Polyethylene oxides
Lipase
Copolymers
Enzymes
Anhydrides
Ethylene Oxide
Dextran
Acids
Dextrans
Conformations
Catalyst activity
Ethylene
Molecules
Oxides

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

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title = "Modification of lipase from Candida rugosa with poly(ethylene oxide-co-maleic anhydride) and its separation using aqueous two-phase partition system",
abstract = "A copolymer was synthesized from polyethylene oxide (PEO) and maleic acid anhydride (MA). Number of ethylene oxide units was varied from 10 to 40. Lipase from Candida nigosa was modified through chemical bonding of MA with amino group of lipase. Degree of modification increased with a decrease in EO unit and increase in copolymer/enzyme ratio. The relative activity of modified enzyme increased with increase in EO unit. It was more than native lipase (100{\%}) when copolymer/enzyme weight ratio was less than 3 for all copolymers. It might be due the conformation change of the lipase molecules on modification that would have exposed the catalytic sites making them more easily accessible. At the highest DM (39{\%}), modified lipase retained more than 50{\%} relative activity. Partitioning of native and modified lipase was also studied by using aqueous two phase synthesized copolymer/dextran system: modified lipase (with EO 30 and 40) showed better separation than the native one. Partition coefficient increased with increase in copolymer/enzyme weight ratio.",
author = "Kwinam Park and Seungmoon Lee and Sanjeev Maken and Wongun Koh and Byoungryul Min and Jinwon Park",
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T1 - Modification of lipase from Candida rugosa with poly(ethylene oxide-co-maleic anhydride) and its separation using aqueous two-phase partition system

AU - Park, Kwinam

AU - Lee, Seungmoon

AU - Maken, Sanjeev

AU - Koh, Wongun

AU - Min, Byoungryul

AU - Park, Jinwon

PY - 2006/7/1

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N2 - A copolymer was synthesized from polyethylene oxide (PEO) and maleic acid anhydride (MA). Number of ethylene oxide units was varied from 10 to 40. Lipase from Candida nigosa was modified through chemical bonding of MA with amino group of lipase. Degree of modification increased with a decrease in EO unit and increase in copolymer/enzyme ratio. The relative activity of modified enzyme increased with increase in EO unit. It was more than native lipase (100%) when copolymer/enzyme weight ratio was less than 3 for all copolymers. It might be due the conformation change of the lipase molecules on modification that would have exposed the catalytic sites making them more easily accessible. At the highest DM (39%), modified lipase retained more than 50% relative activity. Partitioning of native and modified lipase was also studied by using aqueous two phase synthesized copolymer/dextran system: modified lipase (with EO 30 and 40) showed better separation than the native one. Partition coefficient increased with increase in copolymer/enzyme weight ratio.

AB - A copolymer was synthesized from polyethylene oxide (PEO) and maleic acid anhydride (MA). Number of ethylene oxide units was varied from 10 to 40. Lipase from Candida nigosa was modified through chemical bonding of MA with amino group of lipase. Degree of modification increased with a decrease in EO unit and increase in copolymer/enzyme ratio. The relative activity of modified enzyme increased with increase in EO unit. It was more than native lipase (100%) when copolymer/enzyme weight ratio was less than 3 for all copolymers. It might be due the conformation change of the lipase molecules on modification that would have exposed the catalytic sites making them more easily accessible. At the highest DM (39%), modified lipase retained more than 50% relative activity. Partitioning of native and modified lipase was also studied by using aqueous two phase synthesized copolymer/dextran system: modified lipase (with EO 30 and 40) showed better separation than the native one. Partition coefficient increased with increase in copolymer/enzyme weight ratio.

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