Evaluation of an Adsorbent Based on Agricultural Waste (Corn Cobs) for Removal of Tyrosine and Phenylalanine from Aqueous Solutions

Adsorption of phenolic amino acids, such as phenylalanine and tyrosine, is quite relevant for the production of protein hydrolysates used as dietary formulations for patients suffering from congenital disorders of amino acid metabolism, such as phenylketonuria. In this study, an adsorbent prepared f...

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Veröffentlicht in:BioMed research international 2013-01, Vol.2013 (2013), p.1-8
Hauptverfasser: Alves, Cibele C. O., Oliveira, Leandro S., Franca, Adriana S.
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description Adsorption of phenolic amino acids, such as phenylalanine and tyrosine, is quite relevant for the production of protein hydrolysates used as dietary formulations for patients suffering from congenital disorders of amino acid metabolism, such as phenylketonuria. In this study, an adsorbent prepared from corn cobs was evaluated for the removal of tyrosine (Tyr) from both a single component solution and a binary aqueous solution with phenylalanine (Phe). The adsorption behavior of tyrosine was similar to that of phenylalanine in single component solutions, however, with a much lower adsorption capacity (14 mg g−1 for Tyr compared to 109 mg g−1 for Phe). Tyr adsorption kinetics was satisfactorily described by a pseudosecond-order model as it was for Phe. In adsorption equilibrium studies for binary mixtures, the presence of Tyr in Phe solutions favored Phe faster adsorption whereas the opposite behavior was observed for the presence of Phe in Tyr solutions. Such results indicate that, in binary systems, Phe will be adsorbed preferably to Tyr, and this is a welcome feature when employing the prepared adsorbent for the removal of Phe from protein hydrolysates to be used in dietary formulations for phenylketonuria treatment.
doi_str_mv 10.1155/2013/978256
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In adsorption equilibrium studies for binary mixtures, the presence of Tyr in Phe solutions favored Phe faster adsorption whereas the opposite behavior was observed for the presence of Phe in Tyr solutions. Such results indicate that, in binary systems, Phe will be adsorbed preferably to Tyr, and this is a welcome feature when employing the prepared adsorbent for the removal of Phe from protein hydrolysates to be used in dietary formulations for phenylketonuria treatment.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2013/978256</identifier><identifier>PMID: 23936863</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Adsorbents ; Adsorption ; Agricultural pollution ; Agriculture ; Biomedical research ; Costs ; Fourier transforms ; Humans ; Industrial Waste ; Molecular structure ; Phenylalanine - chemistry ; Protein Hydrolysates - chemical synthesis ; Protein Hydrolysates - chemistry ; Proteins ; Solutions - chemistry ; Studies ; Tyrosine - chemistry ; Water - chemistry ; Zea mays - chemistry</subject><ispartof>BioMed research international, 2013-01, Vol.2013 (2013), p.1-8</ispartof><rights>Copyright © 2013 Cibele C. 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The adsorption behavior of tyrosine was similar to that of phenylalanine in single component solutions, however, with a much lower adsorption capacity (14 mg g−1 for Tyr compared to 109 mg g−1 for Phe). Tyr adsorption kinetics was satisfactorily described by a pseudosecond-order model as it was for Phe. In adsorption equilibrium studies for binary mixtures, the presence of Tyr in Phe solutions favored Phe faster adsorption whereas the opposite behavior was observed for the presence of Phe in Tyr solutions. 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O.</au><au>Oliveira, Leandro S.</au><au>Franca, Adriana S.</au><au>Kiran, Ismail</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evaluation of an Adsorbent Based on Agricultural Waste (Corn Cobs) for Removal of Tyrosine and Phenylalanine from Aqueous Solutions</atitle><jtitle>BioMed research international</jtitle><addtitle>Biomed Res Int</addtitle><date>2013-01-01</date><risdate>2013</risdate><volume>2013</volume><issue>2013</issue><spage>1</spage><epage>8</epage><pages>1-8</pages><issn>2314-6133</issn><eissn>2314-6141</eissn><abstract>Adsorption of phenolic amino acids, such as phenylalanine and tyrosine, is quite relevant for the production of protein hydrolysates used as dietary formulations for patients suffering from congenital disorders of amino acid metabolism, such as phenylketonuria. In this study, an adsorbent prepared from corn cobs was evaluated for the removal of tyrosine (Tyr) from both a single component solution and a binary aqueous solution with phenylalanine (Phe). The adsorption behavior of tyrosine was similar to that of phenylalanine in single component solutions, however, with a much lower adsorption capacity (14 mg g−1 for Tyr compared to 109 mg g−1 for Phe). Tyr adsorption kinetics was satisfactorily described by a pseudosecond-order model as it was for Phe. In adsorption equilibrium studies for binary mixtures, the presence of Tyr in Phe solutions favored Phe faster adsorption whereas the opposite behavior was observed for the presence of Phe in Tyr solutions. Such results indicate that, in binary systems, Phe will be adsorbed preferably to Tyr, and this is a welcome feature when employing the prepared adsorbent for the removal of Phe from protein hydrolysates to be used in dietary formulations for phenylketonuria treatment.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>23936863</pmid><doi>10.1155/2013/978256</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
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subjects Adsorbents
Adsorption
Agricultural pollution
Agriculture
Biomedical research
Costs
Fourier transforms
Humans
Industrial Waste
Molecular structure
Phenylalanine - chemistry
Protein Hydrolysates - chemical synthesis
Protein Hydrolysates - chemistry
Proteins
Solutions - chemistry
Studies
Tyrosine - chemistry
Water - chemistry
Zea mays - chemistry
title Evaluation of an Adsorbent Based on Agricultural Waste (Corn Cobs) for Removal of Tyrosine and Phenylalanine from Aqueous Solutions
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