Characteristics of the lipase from Candida rugosa modified with copolymers of polyoxyethylene derivative and maleic acid anhydride

Kwinam Park, Honghyun Kim, Sanjeev Maken, Yeounsoo Kim, Byoung Ryul Min, Jin Won Park

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The hydrophilic copolymer, polyethylene oxide (PEO) allyl ester-maleic anhydride (MA), copolymer was used to modify the lipase from Candida rugosa. MA, in a functional group, reacts easily with amino acids of lipase. The degree of modification (DM) was varied by changing the weight ratio of copolymer to protein of lipase over the range of 10-120 (w/w). The specific activity decreased as DM increased. At the maximum modification degree of 35%, the modified lipase retained more than 65% of the unmodified native lipase activity. The modified lipase displayed a high stability of activity against temperature and pH. The remaining activity of modified lipase was about 2-4 fold of that of native lipase in the severe pH and temperature condition. Finally, it showed 20% greater reaction of substrate at 10 hr than in the case where native lipase was used.

Original languageEnglish
Pages (from-to)412-417
Number of pages6
JournalKorean Journal of Chemical Engineering
Volume22
Issue number3
DOIs
Publication statusPublished - 2005 Jan 1

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Anhydrides
Candida
Lipases
Lipase
Polyethylene glycols
Copolymers
Derivatives
Acids
Maleic Anhydrides
Maleic anhydride
maleic acid
Polyethylene oxides
Functional groups
Amino acids
Esters
Proteins
Amino Acids
Temperature
Substrates

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

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abstract = "The hydrophilic copolymer, polyethylene oxide (PEO) allyl ester-maleic anhydride (MA), copolymer was used to modify the lipase from Candida rugosa. MA, in a functional group, reacts easily with amino acids of lipase. The degree of modification (DM) was varied by changing the weight ratio of copolymer to protein of lipase over the range of 10-120 (w/w). The specific activity decreased as DM increased. At the maximum modification degree of 35{\%}, the modified lipase retained more than 65{\%} of the unmodified native lipase activity. The modified lipase displayed a high stability of activity against temperature and pH. The remaining activity of modified lipase was about 2-4 fold of that of native lipase in the severe pH and temperature condition. Finally, it showed 20{\%} greater reaction of substrate at 10 hr than in the case where native lipase was used.",
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Characteristics of the lipase from Candida rugosa modified with copolymers of polyoxyethylene derivative and maleic acid anhydride. / Park, Kwinam; Kim, Honghyun; Maken, Sanjeev; Kim, Yeounsoo; Min, Byoung Ryul; Park, Jin Won.

In: Korean Journal of Chemical Engineering, Vol. 22, No. 3, 01.01.2005, p. 412-417.

Research output: Contribution to journalArticle

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