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Purification and biochemical characterization of a puromycin-sensitive aminopeptidase from black carp muscle.

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Title: Purification and biochemical characterization of a puromycin-sensitive aminopeptidase from black carp muscle.
Authors: Li, Si-Wei1, Lin, Li-Ping1, Chen, Su-Hua2, Fu, Meng-Yu1, Wu, Guo-Ping1 jdwgp@163.com
Source: Process Biochemistry. Jul2015, Vol. 50 Issue 7, p1061-1067. 7p.
Subjects: Puromycin, Biochemistry, Aminopeptidases, Black carp, Salted fish
Abstract: Exopeptidases such as aminopeptidases and carboxypeptidases are believed to contribute to the formation of free amino acids during postmortem storage and the processing of meat. In order to understand the role of aminopeptidases in the generation of amino acids and formation of flavor compounds in Chinese traditional salted fish, an aminopeptidase was purified and characterized from black carp muscle. The peptide mass fingerprinting of this enzyme suggested that it was a puromycin-sensitive aminopeptidase purified to homogeneity by ammonium sulfate fractionation and three chromatographies. Puromycin was further confirmed as a competitive inhibitor with K i value of 0.25 μM. The 100-kDa enzyme preferentially hydrolyzed substrate Lys-MCA with optimum temperature and pH at 40 °C and 7.5, respectively. At the concentration of 3.2% NaCl and 5% ethanol, the enzyme remained 58.5% and 87.5% of its initial activity, respectively. The aminopeptidase(s) activity decreased slowly and remained 41.1% of its initial activity even after 12 days salting of black carp muscle. These results suggest the possible contribution of fish aminopeptidases to free amino acid formation and flavor generation in Chinese traditional salted fish. [ABSTRACT FROM AUTHOR]
Copyright of Process Biochemistry 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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Header DbId: egs
DbLabel: Engineering Source
An: 102956200
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Purification and biochemical characterization of a puromycin-sensitive aminopeptidase from black carp muscle.
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  Data: <searchLink fieldCode="AR" term="%22Li%2C+Si-Wei%22">Li, Si-Wei</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Lin%2C+Li-Ping%22">Lin, Li-Ping</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Chen%2C+Su-Hua%22">Chen, Su-Hua</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Fu%2C+Meng-Yu%22">Fu, Meng-Yu</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wu%2C+Guo-Ping%22">Wu, Guo-Ping</searchLink><relatesTo>1</relatesTo><i> jdwgp@163.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Process+Biochemistry%22">Process Biochemistry</searchLink>. Jul2015, Vol. 50 Issue 7, p1061-1067. 7p.
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  Data: <searchLink fieldCode="DE" term="%22Puromycin%22">Puromycin</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemistry%22">Biochemistry</searchLink><br /><searchLink fieldCode="DE" term="%22Aminopeptidases%22">Aminopeptidases</searchLink><br /><searchLink fieldCode="DE" term="%22Black+carp%22">Black carp</searchLink><br /><searchLink fieldCode="DE" term="%22Salted+fish%22">Salted fish</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Exopeptidases such as aminopeptidases and carboxypeptidases are believed to contribute to the formation of free amino acids during postmortem storage and the processing of meat. In order to understand the role of aminopeptidases in the generation of amino acids and formation of flavor compounds in Chinese traditional salted fish, an aminopeptidase was purified and characterized from black carp muscle. The peptide mass fingerprinting of this enzyme suggested that it was a puromycin-sensitive aminopeptidase purified to homogeneity by ammonium sulfate fractionation and three chromatographies. Puromycin was further confirmed as a competitive inhibitor with K i value of 0.25 μM. The 100-kDa enzyme preferentially hydrolyzed substrate Lys-MCA with optimum temperature and pH at 40 °C and 7.5, respectively. At the concentration of 3.2% NaCl and 5% ethanol, the enzyme remained 58.5% and 87.5% of its initial activity, respectively. The aminopeptidase(s) activity decreased slowly and remained 41.1% of its initial activity even after 12 days salting of black carp muscle. These results suggest the possible contribution of fish aminopeptidases to free amino acid formation and flavor generation in Chinese traditional salted fish. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Process Biochemistry 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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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.procbio.2015.04.002
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 7
        StartPage: 1061
    Subjects:
      – SubjectFull: Puromycin
        Type: general
      – SubjectFull: Biochemistry
        Type: general
      – SubjectFull: Aminopeptidases
        Type: general
      – SubjectFull: Black carp
        Type: general
      – SubjectFull: Salted fish
        Type: general
    Titles:
      – TitleFull: Purification and biochemical characterization of a puromycin-sensitive aminopeptidase from black carp muscle.
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            NameFull: Li, Si-Wei
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            NameFull: Lin, Li-Ping
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            NameFull: Chen, Su-Hua
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            NameFull: Fu, Meng-Yu
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            NameFull: Wu, Guo-Ping
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            – D: 01
              M: 07
              Text: Jul2015
              Type: published
              Y: 2015
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