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Studying the denaturation of bovine serum albumin by a novel approach of difference-UV analysis.

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Title: Studying the denaturation of bovine serum albumin by a novel approach of difference-UV analysis.
Authors: Nikolaidis, Athanasios1, Moschakis, Thomas1 tmoschak@agro.auth.gr
Source: Food Chemistry. Jan2017, Vol. 215, p235-244. 10p.
Subjects: Denaturation of proteins, Serum albumin, Solution (Chemistry), Food chemistry, Guanidinium chlorides, Clustering of particles
Abstract: A novel approach in the analysis of difference-UV spectrophotometric data for determining the heat denaturation degree of bovine serum albumin (BSA) was assessed. Five different parameters of difference-UV spectra were obtained by subtracting spectra of unheated and denatured protein solutions at different temperature-time combinations. BSA was found to exhibit a maximum degree of heat denaturation of about 17% compared to the complete unfolding caused by 6 M guanidine hydrochloride. This low degree of heat denaturation is probably caused by the aggregation of the initially unfolded protein molecules. The kinetic analysis exhibited discontinuities in the Arrhenius plots, distinguishing the unfolding and aggregation phases of the denaturation process, whereas such a discrimination could not be obtained by differential scanning calorimetry analyses. The proposed method is accurate, fast, simple and sensitive enough to detect changes in the protein heat denaturation even at short temperature-time intervals. [ABSTRACT FROM AUTHOR]
Copyright of Food Chemistry 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: 117497030
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Studying the denaturation of bovine serum albumin by a novel approach of difference-UV analysis.
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  Data: <searchLink fieldCode="AR" term="%22Nikolaidis%2C+Athanasios%22">Nikolaidis, Athanasios</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Moschakis%2C+Thomas%22">Moschakis, Thomas</searchLink><relatesTo>1</relatesTo><i> tmoschak@agro.auth.gr</i>
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  Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. Jan2017, Vol. 215, p235-244. 10p.
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  Data: <searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Serum+albumin%22">Serum albumin</searchLink><br /><searchLink fieldCode="DE" term="%22Solution+%28Chemistry%29%22">Solution (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Food+chemistry%22">Food chemistry</searchLink><br /><searchLink fieldCode="DE" term="%22Guanidinium+chlorides%22">Guanidinium chlorides</searchLink><br /><searchLink fieldCode="DE" term="%22Clustering+of+particles%22">Clustering of particles</searchLink>
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  Data: A novel approach in the analysis of difference-UV spectrophotometric data for determining the heat denaturation degree of bovine serum albumin (BSA) was assessed. Five different parameters of difference-UV spectra were obtained by subtracting spectra of unheated and denatured protein solutions at different temperature-time combinations. BSA was found to exhibit a maximum degree of heat denaturation of about 17% compared to the complete unfolding caused by 6 M guanidine hydrochloride. This low degree of heat denaturation is probably caused by the aggregation of the initially unfolded protein molecules. The kinetic analysis exhibited discontinuities in the Arrhenius plots, distinguishing the unfolding and aggregation phases of the denaturation process, whereas such a discrimination could not be obtained by differential scanning calorimetry analyses. The proposed method is accurate, fast, simple and sensitive enough to detect changes in the protein heat denaturation even at short temperature-time intervals. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Food Chemistry 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:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.foodchem.2016.07.133
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 10
        StartPage: 235
    Subjects:
      – SubjectFull: Denaturation of proteins
        Type: general
      – SubjectFull: Serum albumin
        Type: general
      – SubjectFull: Solution (Chemistry)
        Type: general
      – SubjectFull: Food chemistry
        Type: general
      – SubjectFull: Guanidinium chlorides
        Type: general
      – SubjectFull: Clustering of particles
        Type: general
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      – TitleFull: Studying the denaturation of bovine serum albumin by a novel approach of difference-UV analysis.
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              Text: Jan2017
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              Y: 2017
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              Value: 215
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            – TitleFull: Food Chemistry
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