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Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum)
The utility of the marama bean (MB) as an alternative protein source to soybean (SB) can be limited by the high concentration of trypsin inhibitors (TI). The physical treatment of MB has the potential to ameliorate the antinutritional activities of TI and modify other chemical components. Thus, this...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9317277/ https://www.ncbi.nlm.nih.gov/pubmed/35889324 http://dx.doi.org/10.3390/molecules27144451 |
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author | Alabi, Funmilola Kiarie, Elijah G. Mnisi, Caven Mguvane Mlambo, Victor |
author_facet | Alabi, Funmilola Kiarie, Elijah G. Mnisi, Caven Mguvane Mlambo, Victor |
author_sort | Alabi, Funmilola |
collection | PubMed |
description | The utility of the marama bean (MB) as an alternative protein source to soybean (SB) can be limited by the high concentration of trypsin inhibitors (TI). The physical treatment of MB has the potential to ameliorate the antinutritional activities of TI and modify other chemical components. Thus, this study investigated the effects of physical treatments on the chemical components and trypsin inhibitor activity (TIA) of raw MB and SB. The bean substrates were subjected to each of the following treatment methods: (1) room temperature (20–22 °C) soaking for 24 h; (2) electric stove cooking at 100 °C for 10, 20, and 30 min; (3) steam autoclaving at a temperature of 110 °C and pressure of 7 pounds per square inch (psi), as well as a temperature of 121 °C and 7 psi for 5, 15, and 30 min; (4) pre-soaked autoclaving at 110 °C (7 psi) and 121 °C (17 psi) for 5, 15, and 30 min. Treated MB and SB had greater (p < 0.05) crude protein content than untreated samples. All the treatments (except 24 h soaking of MB) reduced (p < 0.05) the TIA and ash content. Marama and SB are similar in protein content, but their amino acids profile and TIA are quite different. Soaking for 24 h was less effective in reducing TIA in MB and SB, compared to the thermal methods, and it was detrimental to the ash and amino acids profile of the two beans. Soaking prior to autoclaving yielded beans with the lowest TI concentrations. In conclusion, thermal methods reduced the TI contents and modified the level of proximate components and amino acids profile of the beans. |
format | Online Article Text |
id | pubmed-9317277 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93172772022-07-27 Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) Alabi, Funmilola Kiarie, Elijah G. Mnisi, Caven Mguvane Mlambo, Victor Molecules Article The utility of the marama bean (MB) as an alternative protein source to soybean (SB) can be limited by the high concentration of trypsin inhibitors (TI). The physical treatment of MB has the potential to ameliorate the antinutritional activities of TI and modify other chemical components. Thus, this study investigated the effects of physical treatments on the chemical components and trypsin inhibitor activity (TIA) of raw MB and SB. The bean substrates were subjected to each of the following treatment methods: (1) room temperature (20–22 °C) soaking for 24 h; (2) electric stove cooking at 100 °C for 10, 20, and 30 min; (3) steam autoclaving at a temperature of 110 °C and pressure of 7 pounds per square inch (psi), as well as a temperature of 121 °C and 7 psi for 5, 15, and 30 min; (4) pre-soaked autoclaving at 110 °C (7 psi) and 121 °C (17 psi) for 5, 15, and 30 min. Treated MB and SB had greater (p < 0.05) crude protein content than untreated samples. All the treatments (except 24 h soaking of MB) reduced (p < 0.05) the TIA and ash content. Marama and SB are similar in protein content, but their amino acids profile and TIA are quite different. Soaking for 24 h was less effective in reducing TIA in MB and SB, compared to the thermal methods, and it was detrimental to the ash and amino acids profile of the two beans. Soaking prior to autoclaving yielded beans with the lowest TI concentrations. In conclusion, thermal methods reduced the TI contents and modified the level of proximate components and amino acids profile of the beans. MDPI 2022-07-12 /pmc/articles/PMC9317277/ /pubmed/35889324 http://dx.doi.org/10.3390/molecules27144451 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Alabi, Funmilola Kiarie, Elijah G. Mnisi, Caven Mguvane Mlambo, Victor Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title | Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title_full | Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title_fullStr | Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title_full_unstemmed | Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title_short | Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum) |
title_sort | physical treatment reduces trypsin inhibitor activity and modifies chemical composition of marama bean (tylosema esculentum) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9317277/ https://www.ncbi.nlm.nih.gov/pubmed/35889324 http://dx.doi.org/10.3390/molecules27144451 |
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