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Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins
Protein hydrolysis enables production of peptides and free amino acids that are suitable for usage in food and feed or can be used as precursors for bulk chemicals. Several essential amino acids for food and feed have hydrophobic side chains; this property may also be exploited for subsequent separa...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4989023/ https://www.ncbi.nlm.nih.gov/pubmed/27118013 http://dx.doi.org/10.1007/s00253-016-7441-8 |
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author | Widyarani Sari, Yessie W. Ratnaningsih, Enny Sanders, Johan P. M. Bruins, Marieke E. |
author_facet | Widyarani Sari, Yessie W. Ratnaningsih, Enny Sanders, Johan P. M. Bruins, Marieke E. |
author_sort | Widyarani |
collection | PubMed |
description | Protein hydrolysis enables production of peptides and free amino acids that are suitable for usage in food and feed or can be used as precursors for bulk chemicals. Several essential amino acids for food and feed have hydrophobic side chains; this property may also be exploited for subsequent separation. Here, we present methods for selective production of hydrophobic amino acids from proteins. Selectivity can be achieved by selection of starting material, selection of hydrolysis conditions, and separation of achieved hydrolysate. Several protease combinations were applied for hydrolysis of rubber seed protein concentrate, wheat gluten, and bovine serum albumin (BSA). High degree of hydrolysis (>50 %) could be achieved. Hydrophobic selectivity was influenced by the combination of proteases and by the extent of hydrolysis. Combination of Pronase and Peptidase R showed the highest selectivity towards hydrophobic amino acids, roughly doubling the content of hydrophobic amino acids in the products compared to the original substrates. Hydrophobic selectivity of 0.6 mol-hydrophobic/mol-total free amino acids was observed after 6 h hydrolysis of wheat gluten and 24 h hydrolysis of rubber seed proteins and BSA. The results of experiments with rubber seed proteins and wheat gluten suggest that this process can be applied to agro-industrial residues. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00253-016-7441-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4989023 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-49890232016-09-01 Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins Widyarani Sari, Yessie W. Ratnaningsih, Enny Sanders, Johan P. M. Bruins, Marieke E. Appl Microbiol Biotechnol Biotechnological Products and Process Engineering Protein hydrolysis enables production of peptides and free amino acids that are suitable for usage in food and feed or can be used as precursors for bulk chemicals. Several essential amino acids for food and feed have hydrophobic side chains; this property may also be exploited for subsequent separation. Here, we present methods for selective production of hydrophobic amino acids from proteins. Selectivity can be achieved by selection of starting material, selection of hydrolysis conditions, and separation of achieved hydrolysate. Several protease combinations were applied for hydrolysis of rubber seed protein concentrate, wheat gluten, and bovine serum albumin (BSA). High degree of hydrolysis (>50 %) could be achieved. Hydrophobic selectivity was influenced by the combination of proteases and by the extent of hydrolysis. Combination of Pronase and Peptidase R showed the highest selectivity towards hydrophobic amino acids, roughly doubling the content of hydrophobic amino acids in the products compared to the original substrates. Hydrophobic selectivity of 0.6 mol-hydrophobic/mol-total free amino acids was observed after 6 h hydrolysis of wheat gluten and 24 h hydrolysis of rubber seed proteins and BSA. The results of experiments with rubber seed proteins and wheat gluten suggest that this process can be applied to agro-industrial residues. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00253-016-7441-8) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2016-04-27 2016 /pmc/articles/PMC4989023/ /pubmed/27118013 http://dx.doi.org/10.1007/s00253-016-7441-8 Text en © The Author(s) 2016 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Biotechnological Products and Process Engineering Widyarani Sari, Yessie W. Ratnaningsih, Enny Sanders, Johan P. M. Bruins, Marieke E. Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title | Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title_full | Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title_fullStr | Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title_full_unstemmed | Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title_short | Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
title_sort | production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins |
topic | Biotechnological Products and Process Engineering |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4989023/ https://www.ncbi.nlm.nih.gov/pubmed/27118013 http://dx.doi.org/10.1007/s00253-016-7441-8 |
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