Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors
<i>Phaseolus vulgaris</i> α-amylase inhibitor (α-AI) is a protein that has recently gained commercial interest, as it inhibits mammalian α-amylase activity, reducing the absorption of dietary carbohydrates. Numerous studies have reported the efficacy of preparations based on this protein...
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MDPI AG
2023-08-01
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| Series: | Plants |
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| Online Access: | https://www.mdpi.com/2223-7747/12/16/2918 |
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| author | Stefania Peddio Sonia Lorrai Alessandra Padiglia Faustina B. Cannea Tinuccia Dettori Viviana Cristiglio Luigi Genovese Paolo Zucca Antonio Rescigno |
| author_facet | Stefania Peddio Sonia Lorrai Alessandra Padiglia Faustina B. Cannea Tinuccia Dettori Viviana Cristiglio Luigi Genovese Paolo Zucca Antonio Rescigno |
| author_sort | Stefania Peddio |
| collection | DOAJ |
| description | <i>Phaseolus vulgaris</i> α-amylase inhibitor (α-AI) is a protein that has recently gained commercial interest, as it inhibits mammalian α-amylase activity, reducing the absorption of dietary carbohydrates. Numerous studies have reported the efficacy of preparations based on this protein on the control of glycaemic peaks in type-2 diabetes patients and in overweight subjects. A positive influence on microbiota regulation has also been described. In this work, ten insufficiently studied Italian <i>P. vulgaris</i> cultivars were screened for α-amylase- and α-glucosidase-inhibiting activity, as well as for the absence of antinutritional compounds, such as phytohemagglutinin (PHA). All the cultivars presented α-glucosidase-inhibitor activity, while α-AI was missing in two of them. Only the Nieddone cultivar (ACC177) had no haemagglutination activity. In addition, the partial nucleotide sequence of the α-AI gene was identified with the degenerate hybrid oligonucleotide primer (CODEHOP) strategy to identify genetic variability, possibly linked to functional α-AI differences, expression of the α-AI gene, and phylogenetic relationships. Molecular studies showed that α-AI was expressed in all the cultivars, and a close similarity between the Pisu Grogu and Fasolu cultivars’ α-AI and α-AI-4 isoform emerged from the comparison of the partially reconstructed primary structures. Moreover, mechanistic models revealed the interaction network that connects α-AI with the α-amylase enzyme characterized by two interaction hotspots (Asp38 and Tyr186), providing some insights for the analysis of the α-AI primary structure from the different cultivars, particularly regarding the structure–activity relationship. This study can broaden the knowledge about this class of proteins, fuelling the valorisation of Italian agronomic biodiversity through the development of commercial preparations from legume cultivars. |
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| institution | Directory Open Access Journal |
| issn | 2223-7747 |
| language | English |
| last_indexed | 2024-03-10T23:38:42Z |
| publishDate | 2023-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Plants |
| spelling | doaj.art-848876058e2e4bf6bcb127273fa304422023-11-19T02:40:51ZengMDPI AGPlants2223-77472023-08-011216291810.3390/plants12162918Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase InhibitorsStefania Peddio0Sonia Lorrai1Alessandra Padiglia2Faustina B. Cannea3Tinuccia Dettori4Viviana Cristiglio5Luigi Genovese6Paolo Zucca7Antonio Rescigno8Department of Biomedical Sciences (DiSB), University Campus, Monserrato, 09042 Cagliari, ItalyDepartment of Biomedical Sciences (DiSB), University Campus, Monserrato, 09042 Cagliari, ItalyDepartment of Life and Environmental Sciences (DiSVA), University Campus, Monserrato, 09042 Cagliari, ItalyDepartment of Life and Environmental Sciences (DiSVA), University Campus, Monserrato, 09042 Cagliari, ItalyDepartment of Biomedical Sciences (DiSB), University Campus, Monserrato, 09042 Cagliari, ItalyInstitut Laue-Langevin, 38042 Grenoble, FranceCEA/MEM/L-Sim, University Grenoble Alpes, 38044 Grenoble, FranceDepartment of Biomedical Sciences (DiSB), University Campus, Monserrato, 09042 Cagliari, ItalyDepartment of Biomedical Sciences (DiSB), University Campus, Monserrato, 09042 Cagliari, Italy<i>Phaseolus vulgaris</i> α-amylase inhibitor (α-AI) is a protein that has recently gained commercial interest, as it inhibits mammalian α-amylase activity, reducing the absorption of dietary carbohydrates. Numerous studies have reported the efficacy of preparations based on this protein on the control of glycaemic peaks in type-2 diabetes patients and in overweight subjects. A positive influence on microbiota regulation has also been described. In this work, ten insufficiently studied Italian <i>P. vulgaris</i> cultivars were screened for α-amylase- and α-glucosidase-inhibiting activity, as well as for the absence of antinutritional compounds, such as phytohemagglutinin (PHA). All the cultivars presented α-glucosidase-inhibitor activity, while α-AI was missing in two of them. Only the Nieddone cultivar (ACC177) had no haemagglutination activity. In addition, the partial nucleotide sequence of the α-AI gene was identified with the degenerate hybrid oligonucleotide primer (CODEHOP) strategy to identify genetic variability, possibly linked to functional α-AI differences, expression of the α-AI gene, and phylogenetic relationships. Molecular studies showed that α-AI was expressed in all the cultivars, and a close similarity between the Pisu Grogu and Fasolu cultivars’ α-AI and α-AI-4 isoform emerged from the comparison of the partially reconstructed primary structures. Moreover, mechanistic models revealed the interaction network that connects α-AI with the α-amylase enzyme characterized by two interaction hotspots (Asp38 and Tyr186), providing some insights for the analysis of the α-AI primary structure from the different cultivars, particularly regarding the structure–activity relationship. This study can broaden the knowledge about this class of proteins, fuelling the valorisation of Italian agronomic biodiversity through the development of commercial preparations from legume cultivars.https://www.mdpi.com/2223-7747/12/16/2918amylaselow-carb dietbiodiversitybeandiabetesphytohemagglutinin |
| spellingShingle | Stefania Peddio Sonia Lorrai Alessandra Padiglia Faustina B. Cannea Tinuccia Dettori Viviana Cristiglio Luigi Genovese Paolo Zucca Antonio Rescigno Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors Plants amylase low-carb diet biodiversity bean diabetes phytohemagglutinin |
| title | Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors |
| title_full | Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors |
| title_fullStr | Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors |
| title_full_unstemmed | Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors |
| title_short | Biochemical and Phylogenetic Analysis of Italian <i>Phaseolus vulgaris</i> Cultivars as Sources of α-Amylase and α-Glucosidase Inhibitors |
| title_sort | biochemical and phylogenetic analysis of italian i phaseolus vulgaris i cultivars as sources of α amylase and α glucosidase inhibitors |
| topic | amylase low-carb diet biodiversity bean diabetes phytohemagglutinin |
| url | https://www.mdpi.com/2223-7747/12/16/2918 |
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