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Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324

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Title: Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324
Authors: Vatsyayan, Preety1, Kumar, A. Kiran1, Goswami, Papori2, Goswami, Pranab1 pgoswami@iitg.ernet.in
Source: Bioresource Technology. Jan2008, Vol. 99 Issue 1, p68-75. 8p.
Subjects: Cells, Fungi, Filamentous fungi, Molds (Fungi)
Abstract: Abstract: Cytochrome P450 (CYP) monooxygenase activities with different category of substrates namely, alkanes, alkane derivatives, alcohols, aromatic compounds, organic solvents, and steroids were detected in the cells of Aspergillus terreus. High CYP specific activity was observed when methanol (5.6±0.017Umg−1), acetone (7.76±0.02Umg−1), dimethylsulphoxide (DMSO) (9.70±0.005Umg−1), n-hexadecane (4.39±0.02Umg−1), or n-octadecane (4.23±0.01Umg−1) were used as substrates. Significant CYP specific activity was also detected when naphthalene (3.80±0.002Umg−1) was used as substrate. The CYP catalysis of n-hexadecane had followed both terminal and sub terminal oxidations. The activity was localized in the cytosol of n-hexadecane grown cells, while, it was apparently distributed in light mitochondrial fraction and microsomal fraction of glucose grown cells. The substrate specificities of CYP present in all the locations were similar irrespective of the substrates used for the growth. Heme staining of the microsomal fraction containing CYP and other proteins in SDS–PAGE showed single heme protein band with corresponding molecular weight of 110kDa. [Copyright &y& Elsevier]
Copyright of Bioresource Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 26994591
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PubType: Academic Journal
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  Data: Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324
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  Data: <searchLink fieldCode="AR" term="%22Vatsyayan%2C+Preety%22">Vatsyayan, Preety</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kumar%2C+A%2E+Kiran%22">Kumar, A. Kiran</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Goswami%2C+Papori%22">Goswami, Papori</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Goswami%2C+Pranab%22">Goswami, Pranab</searchLink><relatesTo>1</relatesTo><i> pgoswami@iitg.ernet.in</i>
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  Data: <searchLink fieldCode="JN" term="%22Bioresource+Technology%22">Bioresource Technology</searchLink>. Jan2008, Vol. 99 Issue 1, p68-75. 8p.
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  Data: <searchLink fieldCode="DE" term="%22Cells%22">Cells</searchLink><br /><searchLink fieldCode="DE" term="%22Fungi%22">Fungi</searchLink><br /><searchLink fieldCode="DE" term="%22Filamentous+fungi%22">Filamentous fungi</searchLink><br /><searchLink fieldCode="DE" term="%22Molds+%28Fungi%29%22">Molds (Fungi)</searchLink>
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  Data: Abstract: Cytochrome P450 (CYP) monooxygenase activities with different category of substrates namely, alkanes, alkane derivatives, alcohols, aromatic compounds, organic solvents, and steroids were detected in the cells of Aspergillus terreus. High CYP specific activity was observed when methanol (5.6±0.017Umg−1), acetone (7.76±0.02Umg−1), dimethylsulphoxide (DMSO) (9.70±0.005Umg−1), n-hexadecane (4.39±0.02Umg−1), or n-octadecane (4.23±0.01Umg−1) were used as substrates. Significant CYP specific activity was also detected when naphthalene (3.80±0.002Umg−1) was used as substrate. The CYP catalysis of n-hexadecane had followed both terminal and sub terminal oxidations. The activity was localized in the cytosol of n-hexadecane grown cells, while, it was apparently distributed in light mitochondrial fraction and microsomal fraction of glucose grown cells. The substrate specificities of CYP present in all the locations were similar irrespective of the substrates used for the growth. Heme staining of the microsomal fraction containing CYP and other proteins in SDS–PAGE showed single heme protein band with corresponding molecular weight of 110kDa. [Copyright &y& Elsevier]
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  Data: <i>Copyright of Bioresource Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.biortech.2006.11.055
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      – Code: eng
        Text: English
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        Type: general
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      – SubjectFull: Filamentous fungi
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      – TitleFull: Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324
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              Text: Jan2008
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