High voltage atmospheric cold plasma modification of bovine serum albumin
While atmospheric cold plasma has successfully inactivated biohazardous proteinaceous molecules (unwanted enzymes, prions, and allergens) and modified proteins with improved functionality, few studies have characterized plasma-protein interactions. This study investigates the physicochemical interac...
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| Published in: | Food science & technology Vol. 149; p. 111995 |
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| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
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Elsevier Ltd
01-09-2021
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| Abstract | While atmospheric cold plasma has successfully inactivated biohazardous proteinaceous molecules (unwanted enzymes, prions, and allergens) and modified proteins with improved functionality, few studies have characterized plasma-protein interactions. This study investigates the physicochemical interactions, structural alteration, and reaction mechanisms of bovine serum albumin (BSA) subjected to high voltage atmospheric cold plasma (HVACP) generated by a dielectric barrier discharge in sealed bags packed with air or modified air (65% O2, 30% N2, 5% CO2). Treating 10 mL of BSA solution (50 mg/mL) with HVACP for 60 min changed the sample from transparent to yellow and induced protein precipitation. HVACP also induced protein unfolding, altered secondary structure (27% loss of α-helix), and increased disorder structure (10% increase of random coil). HVACP-treated protein increased in average size from 10 nm to 113 μm, with a broader size distribution after 60 min of HVACP treatment. SDS-PAGE and mass spectrometry showed the formation of new peptides from 1 to 10 kDa, indicating plasma-triggered peptide bond cleavage. Chemical analysis and mass spectrometry demonstrated oxidation and deamidation in HVACP-treated samples. This study illustrates that interactions between HVACP-induced reactive species and proteins may introduce structural alterations, protein aggregation, peptide cleavage, and side-group modifications to proteins in aqueous conditions.
High voltage atmospheric cold plasma (HVACP) induces protein structure changes.HVACP induced side-group modifications, such as oxidation and deamidation.HVACP induced protein unfolding, denaturation, aggregation, and precipitation.HVACP-triggered peptide bond cleavage generated new peptides from 1 to 10 kDa. |
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| AbstractList | While atmospheric cold plasma has successfully inactivated biohazardous proteinaceous molecules (unwanted enzymes, prions, and allergens) and modified proteins with improved functionality, few studies have characterized plasma-protein interactions. This study investigates the physicochemical interactions, structural alteration, and reaction mechanisms of bovine serum albumin (BSA) subjected to high voltage atmospheric cold plasma (HVACP) generated by a dielectric barrier discharge in sealed bags packed with air or modified air (65% O2, 30% N2, 5% CO2). Treating 10 mL of BSA solution (50 mg/mL) with HVACP for 60 min changed the sample from transparent to yellow and induced protein precipitation. HVACP also induced protein unfolding, altered secondary structure (27% loss of α-helix), and increased disorder structure (10% increase of random coil). HVACP-treated protein increased in average size from 10 nm to 113 μm, with a broader size distribution after 60 min of HVACP treatment. SDS-PAGE and mass spectrometry showed the formation of new peptides from 1 to 10 kDa, indicating plasma-triggered peptide bond cleavage. Chemical analysis and mass spectrometry demonstrated oxidation and deamidation in HVACP-treated samples. This study illustrates that interactions between HVACP-induced reactive species and proteins may introduce structural alterations, protein aggregation, peptide cleavage, and side-group modifications to proteins in aqueous conditions.
High voltage atmospheric cold plasma (HVACP) induces protein structure changes.HVACP induced side-group modifications, such as oxidation and deamidation.HVACP induced protein unfolding, denaturation, aggregation, and precipitation.HVACP-triggered peptide bond cleavage generated new peptides from 1 to 10 kDa. |
| ArticleNumber | 111995 |
| Author | Hou, Hu Xu, Lei Garner, Allen L. Farkas, Brian Keener, Kevin M. Tao, Bernard |
| Author_xml | – sequence: 1 givenname: Lei orcidid: 0000-0001-8280-3162 surname: Xu fullname: Xu, Lei organization: Department of Food Science, Purdue University, West Lafayette, IN, 47907, USA – sequence: 2 givenname: Hu surname: Hou fullname: Hou, Hu organization: College of Food Science and Engineering, Ocean University of China, Qingdao, Shandong Province, 266003, China – sequence: 3 givenname: Brian surname: Farkas fullname: Farkas, Brian organization: Department of Food Science, Purdue University, West Lafayette, IN, 47907, USA – sequence: 4 givenname: Kevin M. orcidid: 0000-0001-9873-9353 surname: Keener fullname: Keener, Kevin M. organization: School of Engineering, University of Guelph, Guelph, Ontario, N1G 2W1, Canada – sequence: 5 givenname: Allen L. orcidid: 0000-0001-5416-7437 surname: Garner fullname: Garner, Allen L. email: algarner@purdue.edu organization: School of Nuclear Engineering, Purdue University, West Lafayette, IN, 47906, USA – sequence: 6 givenname: Bernard surname: Tao fullname: Tao, Bernard email: tao@purdue.edu organization: Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, IN, 47907, USA |
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