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Microsome-bound alcohol oxidase catalyzed production of carbonyl compounds from alcohol substrates

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바이오화학분류
    • 바이오정밀화학
      1. 용매
      2. 화학제품
    • 화장품용 기능성소재
      1. 계면활성제⁄증점제
    • 의료용 화학소재
      1. 치료제
      2. 식품첨가제
논문

Microsome-bound alcohol oxidase catalyzed production of carbonyl compounds from alcohol substrates

학술지

Journal of molecular catalysis. B, Enzymatic

저자명

Kakoti, Ankana; Kumar, Adepu Kiran; Goswami, Pranab

초록

<P><B>Graphical abstract</B></P><P><ce:figure id='fig0005'></ce:figure></P><P><B>Highlights</B></P><P>&#x025BA; High yield production of carbonyl compounds using microsome-bound AOx catalyses was established. &#x025BA; The AOx catalyzed production of carbonyls was achieved in environmentally benign conditions. &#x025BA; The microsome bound AOx was successfully immobilized in polyurethane foam matrix. &#x025BA; The synthesis of industrially important <I>n</I>-heptanal was achieved by polyurethane foam immobilized AOx catalytic process. &#x025BA; High operational stability of the immobilized enzyme was demonstrated.</P> <P><B>Abstract</B></P><P>High yield conversion of a wide range of alcohol substrates to their corresponding aldehydes was demonstrated using a microsomal alcohol oxidase (AOx) from <I>Aspergillus terreus</I>. The microsome bound AOx preparation was then immobilized into polyurethane foam matrix following a simple adsorption technique. The successful immobilization of the enzyme into the foam matrix was demonstrated microscopically and by biological staining. The enzyme loading was measured as &sim;2.02Umg<SUP>&minus;1</SUP> (76.6mgprotein %) of polyurethane foam. The optimum activity of the immobilized enzyme was detected in the pH range 7.0&ndash;8.0. The catalytic activity of the immobilized AOx was utilized for the production of <I>n</I>-heptanal. A maximum <I>n</I>-heptanal yield of 20.7&plusmn;1.2% (w/w) was achieved at a substrate concentration of 10mM <I>n</I>-heptanol; beyond this concentration substrate dependent inhibition of the catalytic reaction was observed. The operational stability of the immobilized enzyme was determined and found to be &sim;60% of the initial activity till the fifth reaction cycle, thus providing high cumulative yield of the product. The deactivation (<I>k</I><SUB><I>d</I></SUB>) and half-life time (<I>t</I><SUB>1/2</SUB>) of the immobilized enzyme were 5.17&times;10<SUP>&minus;5</SUP>min<SUP>&minus;1</SUP> and &sim;9days, respectively. The results demonstrated the potential application of the polyurethane foam immobilized microsomal AOx-based environmentally benign biocatalytic process for the production of industrially important <I>n</I>-heptanal.</P>

발행연도

2012

ISSN

1381-1177

ISSN

1873-3158

78

페이지

pp.98-104

주제어

Aspergillus terreus; Alcohol oxidase; Enzyme catalysis; Alcohols; Carbonyl compounds

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1 2023-12-11
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논문; 2012-06-01

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