Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
[Display omitted] •Oat protein treated by alcalase and flavourzyme is a good source of antidiabetic peptides.•Oat peptides can inhibit three of the main glucose regulating enzymes: α-amylase, α-glucosidase, and DPP-IV.•Ultrafiltration and RP-HPLC fractionation enhanced the antidiabetic effect of oat...
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Published in | Journal of functional foods Vol. 87; p. 104829 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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Elsevier Ltd
01.12.2021
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Abstract | [Display omitted]
•Oat protein treated by alcalase and flavourzyme is a good source of antidiabetic peptides.•Oat peptides can inhibit three of the main glucose regulating enzymes: α-amylase, α-glucosidase, and DPP-IV.•Ultrafiltration and RP-HPLC fractionation enhanced the antidiabetic effect of oat peptides.•LC-MS/MS analysis displayed in total 27 de novo sequences from the most effective fractions.
The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme fractionated into different molecular weights and hydrophobicity, indicated that the relatively hydrophobic fraction of 1–5 kDa inhibited enzymes related to glucose digestion, absorption, and metabolism activities. The α-amylase and DPP-IV were inhibited 57 and 78%, respectively, even at low peptide concentrations. LC-MS/MS analysis of the most effective fractions disclosed two eight amino acid sequences, identified from 12S oat globulin (GDVVALPA and DVVALPAG), and other sequences rich in amino acids like proline, leucine, valine, phenylalanine, and glutamine. The results suggest that proline and hydrophobic amino acids may favor hydrophobic interactions and hydrogen bonding with the target enzymes, especially the Leu-Pro sequence found in potent DPP-IV inhibitors. |
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AbstractList | [Display omitted]
•Oat protein treated by alcalase and flavourzyme is a good source of antidiabetic peptides.•Oat peptides can inhibit three of the main glucose regulating enzymes: α-amylase, α-glucosidase, and DPP-IV.•Ultrafiltration and RP-HPLC fractionation enhanced the antidiabetic effect of oat peptides.•LC-MS/MS analysis displayed in total 27 de novo sequences from the most effective fractions.
The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme fractionated into different molecular weights and hydrophobicity, indicated that the relatively hydrophobic fraction of 1–5 kDa inhibited enzymes related to glucose digestion, absorption, and metabolism activities. The α-amylase and DPP-IV were inhibited 57 and 78%, respectively, even at low peptide concentrations. LC-MS/MS analysis of the most effective fractions disclosed two eight amino acid sequences, identified from 12S oat globulin (GDVVALPA and DVVALPAG), and other sequences rich in amino acids like proline, leucine, valine, phenylalanine, and glutamine. The results suggest that proline and hydrophobic amino acids may favor hydrophobic interactions and hydrogen bonding with the target enzymes, especially the Leu-Pro sequence found in potent DPP-IV inhibitors. The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme fractionated into different molecular weights and hydrophobicity, indicated that the relatively hydrophobic fraction of 1–5 kDa inhibited enzymes related to glucose digestion, absorption, and metabolism activities. The α-amylase and DPP-IV were inhibited 57 and 78%, respectively, even at low peptide concentrations. LC-MS/MS analysis of the most effective fractions disclosed two eight amino acid sequences, identified from 12S oat globulin (GDVVALPA and DVVALPAG), and other sequences rich in amino acids like proline, leucine, valine, phenylalanine, and glutamine. The results suggest that proline and hydrophobic amino acids may favor hydrophobic interactions and hydrogen bonding with the target enzymes, especially the Leu-Pro sequence found in potent DPP-IV inhibitors. |
ArticleNumber | 104829 |
Author | Richard, Caroline Chen, Lingyun Ramírez Fuentes, Lourdes |
Author_xml | – sequence: 1 givenname: Lourdes surname: Ramírez Fuentes fullname: Ramírez Fuentes, Lourdes – sequence: 2 givenname: Caroline surname: Richard fullname: Richard, Caroline – sequence: 3 givenname: Lingyun surname: Chen fullname: Chen, Lingyun email: lingyun.chen@ualberta.ca |
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Cites_doi | 10.1111/j.1745-4514.1978.tb00184.x 10.1007/s13749-014-0052-z 10.1007/s00394-015-0974-2 10.1016/j.jff.2017.12.061 10.1007/s12013-014-9998-0 10.5001/omj.2012.68 10.1111/cbdd.13105 10.7164/antibiotics.37.422 10.1111/jfbc.12451 10.1155/2016/8216378 10.22364/eeb.14.23 10.3390/antiox9060557 10.1016/j.foodchem.2012.06.088 10.1016/j.bbrc.2013.03.010 10.1016/j.ijbiomac.2020.10.060 10.1039/c3fo60262a 10.3390/ijms19102883 10.1111/ijfs.14087 10.1016/j.foodres.2013.11.038 10.1016/j.foodchem.2018.11.110 10.1021/jf9018245 10.1039/C6FO01411A 10.1021/acs.jafc.5b04016 10.1006/abbi.1999.1423 10.1039/9781847557698 10.1271/bbb.68.1858 10.1007/s00394-008-0710-2 10.1094/9781891127649.008 10.1002/biof.1219 10.1271/bbb.61.1138 10.1111/jfbc.12518 10.1016/j.foodchem.2013.04.123 10.1515/znc-1999-3-417 10.1016/j.foodchem.2013.08.097 10.1021/acs.jafc.8b00960 10.1021/jf900135e 10.1016/j.foodchem.2015.08.058 10.1016/j.lwt.2011.04.002 10.1093/jxb/34.10.1320 10.1016/j.jff.2016.07.024 10.18433/J35S3K 10.2174/1573399815666190618093315 10.1111/dme.14358 10.1016/j.foodchem.2012.02.183 10.20960/nh.1713 10.1016/j.foodchem.2012.08.032 10.1016/j.foodchem.2015.05.120 10.1016/j.beem.2007.07.005 10.1016/j.jff.2016.09.001 10.1271/bbb.110137 10.1186/s12913-019-4384-7 10.1089/ind.2018.0032 10.2135/cropsci2010.09.0548 10.3390/ijms20235978 10.1016/j.jff.2014.09.010 10.1007/s13300-013-0034-y 10.1016/j.foodres.2015.07.046 10.1007/s11694-019-00296-0 |
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Keywords | Antidiabetic peptides DPP-IV inhibition Type 2 diabetes Peptide sequencing α-amylase inhibition Oat protein |
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References | Van Smoorenburg, Hertroijs, Dekkers, Elissen, Melles (b0275) 2019; 19 Esfandi, R., Willmore, W. G., & Tsopmo, A. (2018). González-Montoya, Hernández-Ledesma, Mora-Escobedo, Martínez-Villaluenga (b0070) 2018; 19 Tacias-Pascacio, Morellon-Sterling, Siar, Tavano, Berenguer-Murcia, Fernandez-Lafuente (b0260) 2020; 165 Chakraborty, Hsu, Agoramoorthy (b0035) 2014; 70 Oseguera Toledo, Gonzalez de Mejia, Sivaguru, Amaya-Llano (b0215) 2016; 27 (pp. 123–142). Burgess, S. R., Shewry, P. R., Matlashewski, G. J., Altosaar, I., & Miflin, B. J. (1983). Characteristics Of Oat (Avena sativa L.) Seed Globulins. In Ahrén (b0010) 2007; 21 Liu, Li, Shi, Wang, Chen, Liu, Huang (b0130) 2009; 57 Cheung, Nakayama, Hsu, Samaranayaka, Li-Chan (b0040) 2009; 57 Gao, Kawabata (b0060) 2014; 68 Nongonierma, A. B., & Fitzgerald, R. J. (2013). Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing casein-derived peptides. https://doi.org/10.1016/j.jff.2013.09.012. Sosa Crespo, Laviada Molina, Chel-Guerrero, Ortiz-Andrade, Betancur-Ancona (b0255) 2018; 35 Bashary, Vyas, Nayak, Suttee, Verma, Narang, Khatik (b0025) 2019; 16 García-Pérez, Álvarez, Dilla, Gil-Guillén, Orozco-Beltrán (b0065) 2013; 4 Shai, Magano, Lebelo, Mogale (b0245) 2011; 5 de Sales, de Souza, Simeoni, Magalhães, Silveira (b0045) 2012; 15 Huang, Hung, Jao, Tung, Hsu (b0085) 2014; 11 Nieto-Nieto, Wang, Ozimek, Chen (b0170) 2014; 55 Kwon, Vattem, Shetty (b0115) 2006; 15 Peterson, D. M. (2011). Storage Proteins. In Rubi, Campos, Peralta González, Guerrero, Ancona (b0240) 2013; 2013 Tiefenbacher (b0265) 2017 Lacroix, I. M. E., Chen, X.-M., Kitts, D. D., & Li-Chan, E. C. Y. (2017). Investigation into the bioavailability of milk protein-derived peptides with dipeptidyl-peptidase IV inhibitory activity using Caco-2 cell monolayers 8, 701. https://doi.org/10.1039/c6fo01411a. Retrieved from 515. (Vol. 34). Retrieved from https://academic.oup.com/jxb/article/34/10/1320/497818. . Ngoh, Gan (b0165) 2016; 190 Oseguera-Toledo, Gonzalez de Mejia, Amaya-Llano (b0205) 2015; 76 Dickinson, E., & Leser, M. E. (2007). Wang, Yu, Zhang, Zhang, Fan (b0300) 2015; 63 Admassu, Gasmalla, Yang, Zhao (b0005) 2018; 66 Kim, Lee, Lee, Lee, Baek, Kim, Park (b0110) 1999; 371 Walters, Willmore, Tsopmo (b0290) 2020; 9 Minkiewicz, Iwaniak, Darewicz (b0145) 2019; 20 Ren, Liang, Jin, Zhang, Chen, Wu, Lai (b0235) 2016; 26 Awosika, Aluko (b0020) 2019; 54 Nongonierma, A. B., & Fitzgerald, R. J. (2014). Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. https://doi.org/10.1016/j.foodchem.2013.08.097. Lebovitz, H. E., Irl Hirsch, M. R., & Vassello, J. (1997). Xu, Galanopoulos, Sismour, Ren, Mersha, Lynch, Almutaimi (b0315) 2020; 14 Nabeno, M., Akahoshi, F., Kishida, H., Miyaguchi, I., Tanaka, Y., Ishii, S., & Kadowaki, T. (2013). A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site. Velarde-Salcedo, Barrera-Pacheco, Lara-González, Montero-Morán, Díaz-Gois, González De Mejia, Barba De La Rosa (b0285) 2013; 136 Yan, Fetch, Frégeau-Reid, Rossnagel, Ames (b0320) 2011; 51 IDF Diabetes Atlas 9th edition. (2019). IDF Diabetes Atlas 9th edition 2019. In Hatanaka, Inoue, Arima, Kumagai, Usuki, Kawakami, Mukaihara (b0075) 2012; 134 Moon, Islam, Ahn, Chowdhury, Sohn, Jung, Choi (b0155) 2011; 75 Jhong, Riyaphan, Lin, Chia, Weng (b0100) 2015; 41 Nongonierma, FitzGerald (b0190) 2019; 43 Umezawa, Aoyagi, Ogawa, Naganawa, Hamada, Takeuchi (b0270) 1984; 37 Orsini Delgado, Tironi, Añón (b0200) 2011; 44 Lordan, Smyth, Soler-Vila, Stanton, Paul Ross (b0135) 2013; 141 Nishioka, Watanabe, Kawabata, Niki (b0175) 1997; 61 Vanvi, Tsopmo (b0280) 2016; 2016 Ibrahim, Bester, Neitz, Gaspar (b0090) 2018; 91 Patil, Mandal, Tomar, Anand (b0220) 2015; 54 Hopkins, Andrews, Salem, Taylor, Roux, Robertson, Burns (b0080) 2020; 37 Wang, Du, Fang, Liu, Min, Liu (b0310) 2018; 42 Kannan, Hettiarachchy, Marshall (b0105) 2011 Matsui, Oki, Osajima (b0140) 1999; 54 Arise (b0015) 2016; 14 Möller, Scholz-Ahrens, Roos, Schrezenmeir (b0150) 2008; 47 Oseguera-Toledo, González de Mejía, Reynoso-Camacho, Cardador-Martínez, Amaya-Llano (b0210) 2014; 13 Powers, Whitaker (b0230) 1978; 1 Wang, Zhang, Yu, He, Cui, Wang, Fan (b0305) 2018; 42 Olokoba, Obateru, Olokoba (b0195) 2012; 27 Wang, F., Yu, G., Zhang, Y., Zhang, B., & Fan, J. (2015a). Dipeptidyl Peptidase IV Inhibitory Peptides Derived from Oat (Avena sativa L.), Buckwheat (Fagopyrum esculentum), and Highland Barley (Hordeum vulgare trif urcatum (L.) Trofim) Proteins. Yu, Wang, Zhang, Fan (b0325) 2016; 194 Yu, Yin, Zhao, Liu, Chen (b0330) 2012; 135 Sharma, Gat, Arya, Kumar, Panghal, Kumar (b0250) 2019; 15 Hopkins (10.1016/j.jff.2021.104829_b0080) 2020; 37 Ngoh (10.1016/j.jff.2021.104829_b0165) 2016; 190 Ahrén (10.1016/j.jff.2021.104829_b0010) 2007; 21 Nongonierma (10.1016/j.jff.2021.104829_b0190) 2019; 43 Möller (10.1016/j.jff.2021.104829_b0150) 2008; 47 Sosa Crespo (10.1016/j.jff.2021.104829_b0255) 2018; 35 Jhong (10.1016/j.jff.2021.104829_b0100) 2015; 41 González-Montoya (10.1016/j.jff.2021.104829_b0070) 2018; 19 Oseguera-Toledo (10.1016/j.jff.2021.104829_b0205) 2015; 76 Ren (10.1016/j.jff.2021.104829_b0235) 2016; 26 Cheung (10.1016/j.jff.2021.104829_b0040) 2009; 57 Nieto-Nieto (10.1016/j.jff.2021.104829_b0170) 2014; 55 10.1016/j.jff.2021.104829_b0030 Huang (10.1016/j.jff.2021.104829_b0085) 2014; 11 Arise (10.1016/j.jff.2021.104829_b0015) 2016; 14 Ibrahim (10.1016/j.jff.2021.104829_b0090) 2018; 91 Hatanaka (10.1016/j.jff.2021.104829_b0075) 2012; 134 Admassu (10.1016/j.jff.2021.104829_b0005) 2018; 66 Walters (10.1016/j.jff.2021.104829_b0290) 2020; 9 10.1016/j.jff.2021.104829_b0120 Orsini Delgado (10.1016/j.jff.2021.104829_b0200) 2011; 44 Yu (10.1016/j.jff.2021.104829_b0330) 2012; 135 García-Pérez (10.1016/j.jff.2021.104829_b0065) 2013; 4 Kwon (10.1016/j.jff.2021.104829_b0115) 2006; 15 10.1016/j.jff.2021.104829_b0125 Oseguera Toledo (10.1016/j.jff.2021.104829_b0215) 2016; 27 Chakraborty (10.1016/j.jff.2021.104829_b0035) 2014; 70 10.1016/j.jff.2021.104829_b0160 Xu (10.1016/j.jff.2021.104829_b0315) 2020; 14 Yan (10.1016/j.jff.2021.104829_b0320) 2011; 51 Patil (10.1016/j.jff.2021.104829_b0220) 2015; 54 Van Smoorenburg (10.1016/j.jff.2021.104829_b0275) 2019; 19 Awosika (10.1016/j.jff.2021.104829_b0020) 2019; 54 Matsui (10.1016/j.jff.2021.104829_b0140) 1999; 54 Rubi (10.1016/j.jff.2021.104829_b0240) 2013; 2013 Kim (10.1016/j.jff.2021.104829_b0110) 1999; 371 Shai (10.1016/j.jff.2021.104829_b0245) 2011; 5 Sharma (10.1016/j.jff.2021.104829_b0250) 2019; 15 Tiefenbacher (10.1016/j.jff.2021.104829_b0265) 2017 10.1016/j.jff.2021.104829_b0295 Wang (10.1016/j.jff.2021.104829_b0305) 2018; 42 10.1016/j.jff.2021.104829_b0055 Liu (10.1016/j.jff.2021.104829_b0130) 2009; 57 Tacias-Pascacio (10.1016/j.jff.2021.104829_b0260) 2020; 165 Nishioka (10.1016/j.jff.2021.104829_b0175) 1997; 61 Bashary (10.1016/j.jff.2021.104829_b0025) 2019; 16 10.1016/j.jff.2021.104829_b0050 10.1016/j.jff.2021.104829_b0095 Wang (10.1016/j.jff.2021.104829_b0300) 2015; 63 Lordan (10.1016/j.jff.2021.104829_b0135) 2013; 141 Yu (10.1016/j.jff.2021.104829_b0325) 2016; 194 Velarde-Salcedo (10.1016/j.jff.2021.104829_b0285) 2013; 136 Powers (10.1016/j.jff.2021.104829_b0230) 1978; 1 Oseguera-Toledo (10.1016/j.jff.2021.104829_b0210) 2014; 13 10.1016/j.jff.2021.104829_b0185 Wang (10.1016/j.jff.2021.104829_b0310) 2018; 42 de Sales (10.1016/j.jff.2021.104829_b0045) 2012; 15 Olokoba (10.1016/j.jff.2021.104829_b0195) 2012; 27 10.1016/j.jff.2021.104829_b0225 Umezawa (10.1016/j.jff.2021.104829_b0270) 1984; 37 Moon (10.1016/j.jff.2021.104829_b0155) 2011; 75 10.1016/j.jff.2021.104829_b0180 Kannan (10.1016/j.jff.2021.104829_b0105) 2011 Gao (10.1016/j.jff.2021.104829_b0060) 2014; 68 Minkiewicz (10.1016/j.jff.2021.104829_b0145) 2019; 20 Vanvi (10.1016/j.jff.2021.104829_b0280) 2016; 2016 |
References_xml | – volume: 68 start-page: 1858 year: 2014 end-page: 1864 ident: b0060 article-title: Importance of the B Ring and Its Substitution on the α-Glucosidase Inhibitory Activity of Baicalein, 5,6,7-Trihydroxyflavone Hong GAO & Jun KAWABATA publication-title: Bioscience, Biotechnology, and Biochemistry contributor: fullname: Kawabata – volume: 15 start-page: 69 year: 2019 end-page: 78 ident: b0250 article-title: A review on microbial alkaline protease: An essential tool for various industrial approaches publication-title: Industrial Biotechnology contributor: fullname: Kumar – volume: 61 start-page: 1138 year: 1997 end-page: 1141 ident: b0175 article-title: Isolation and Activity of N-p-Coumaroyltyramine, an α-Glucosidase Inhibitor in Welsh Onion (Allium fistulosum) publication-title: Bioscience, Biotechnology, and Biochemistry contributor: fullname: Niki – volume: 21 start-page: 517 year: 2007 end-page: 533 ident: b0010 article-title: DPP-4 inhibitors publication-title: Best Practice and Research in Clinical Endocrinology and Metabolism contributor: fullname: Ahrén – volume: 54 start-page: 259 year: 1999 end-page: 263 ident: b0140 article-title: Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate publication-title: Zeitschrift Fur Naturforschung - Section C Journal of Biosciences contributor: fullname: Osajima – volume: 37 start-page: 422 year: 1984 end-page: 425 ident: b0270 article-title: Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria publication-title: The Journal of Antibiotics contributor: fullname: Takeuchi – volume: 136 start-page: 758 year: 2013 end-page: 764 ident: b0285 article-title: In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins publication-title: Food Chemistry contributor: fullname: Barba De La Rosa – volume: 4 start-page: 175 year: 2013 end-page: 194 ident: b0065 article-title: Adherence to therapies in patients with type 2 diabetes publication-title: Diabetes Therapy contributor: fullname: Orozco-Beltrán – volume: 13 start-page: 147 year: 2014 end-page: 157 ident: b0210 article-title: Proteins and bioactive peptides publication-title: Nutrafoods contributor: fullname: Amaya-Llano – volume: 16 start-page: 117 year: 2019 end-page: 136 ident: b0025 article-title: An Insight of Alpha-amylase Inhibitors as a Valuable Tool in the Management of Type 2 Diabetes Mellitus publication-title: Current Diabetes Reviews contributor: fullname: Khatik – volume: 194 start-page: 577 year: 2016 end-page: 586 ident: b0325 article-title: In vitro inhibition of platelet aggregation by peptides derived from oat (Avena sativa L.), highland barley (Hordeum vulgare Linn. var. nudum Hook. f.), and buckwheat (Fagopyrum esculentum Moench) proteins publication-title: Food Chemistry contributor: fullname: Fan – volume: 66 start-page: 4872 year: 2018 end-page: 4882 ident: b0005 article-title: Identification of Bioactive Peptides with α-Amylase Inhibitory Potential from Enzymatic Protein Hydrolysates of Red Seaweed (Porphyra spp) [Research-article] publication-title: Journal of Agricultural and Food Chemistry contributor: fullname: Zhao – volume: 26 start-page: 439 year: 2016 end-page: 450 ident: b0235 article-title: Identification and characterization of two novel α-glucosidase inhibitory oligopeptides from hemp (Cannabis sativa L.) seed protein publication-title: Journal of Functional Foods contributor: fullname: Lai – volume: 2016 start-page: 1 year: 2016 end-page: 8 ident: b0280 article-title: Pepsin digested oat bran proteins: Separation, antioxidant activity, and identification of new peptides publication-title: Journal of Chemistry contributor: fullname: Tsopmo – volume: 20 start-page: 5978 year: 2019 ident: b0145 article-title: BIOPEP-UWM database of bioactive peptides: Current opportunities publication-title: International Journal of Molecular Sciences contributor: fullname: Darewicz – volume: 14 start-page: 163 year: 2016 end-page: 172 ident: b0015 article-title: In vitro antioxidant and α-amylase inhibitory properties of watermelon seed protein hydrolysates publication-title: Environmental and Experimental Biology contributor: fullname: Arise – volume: 42 start-page: 12 year: 2018 end-page: 20 ident: b0305 article-title: Oat globulin peptides regulate antidiabetic drug targets and glucose transporters in Caco-2 cells publication-title: Journal of Functional Foods contributor: fullname: Fan – volume: 44 start-page: 1752 year: 2011 end-page: 1760 ident: b0200 article-title: Antioxidant activity of amaranth protein or their hydrolysates under simulated gastrointestinal digestion publication-title: LWT - Food Science and Technology contributor: fullname: Añón – volume: 75 start-page: 1472 year: 2011 end-page: 1480 ident: b0155 article-title: Protein Tyrosine Phosphatase 1B and α-Glucosidase Inhibitory Phlorotannins from Edible Brown Algae, Ecklonia stolonifera and Eiseniaï¿¿bicyclis publication-title: Biotechnology and Biochemistry contributor: fullname: Choi – volume: 2013 year: 2013 ident: b0240 article-title: Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis publication-title: International Journal of Food Science contributor: fullname: Ancona – start-page: 15 year: 2017 end-page: 121 ident: b0265 article-title: Technology of main ingredients—Water and flours publication-title: Wafer and Waffle contributor: fullname: Tiefenbacher – volume: 55 start-page: 418 year: 2014 end-page: 425 ident: b0170 article-title: Effects of partial hydrolysis on structure and gelling properties of oat globular proteins publication-title: Food Research International contributor: fullname: Chen – start-page: 1 year: 2011 end-page: 28 ident: b0105 publication-title: Bioactive Food Proteins and Peptides: Applications in Human Health contributor: fullname: Marshall – volume: 42 start-page: 1 year: 2018 end-page: 10 ident: b0310 article-title: Evaluation of the antidiabetic activity of hydrolyzed peptides derived from Juglans mandshurica Maxim. fruits in insulin-resistant HepG2 cells and type 2 diabetic mice publication-title: Journal of Food Biochemistry contributor: fullname: Liu – volume: 15 start-page: 141 year: 2012 end-page: 183 ident: b0045 article-title: α-amylase inhibitors: A review of raw material and isolated compounds from plant source publication-title: Journal of Pharmacy and Pharmaceutical Sciences contributor: fullname: Silveira – volume: 57 start-page: 9234 year: 2009 end-page: 9242 ident: b0040 article-title: Angiotensin-I Converting Enzyme Inhibitory Activity of Hydrolysates from Oat (Avena sativa) Proteins by In Silico and In Vitro Analyses publication-title: Journal of Agricultural and Food Chemistry contributor: fullname: Li-Chan – volume: 19 year: 2019 ident: b0275 article-title: Patients’ perspective on self-management: Type 2 diabetes in daily life publication-title: BMC Health Services Research contributor: fullname: Melles – volume: 37 start-page: 1944 year: 2020 end-page: 1950 ident: b0080 article-title: Improving understanding of type 2 diabetes remission: research recommendations from Diabetes UK’s 2019 remission workshop publication-title: Diabetic Medicine contributor: fullname: Burns – volume: 5 start-page: 2863 year: 2011 end-page: 2867 ident: b0245 article-title: Inhibitory effects of five medicinal plants on rat alpha-glucosidase: Comparison with their effects on yeast alpha-glucosidase publication-title: Journal of Medicinal Plants Research contributor: fullname: Mogale – volume: 70 start-page: 907 year: 2014 end-page: 922 ident: b0035 article-title: Understanding the molecular dynamics of type-2 diabetes drug target DPP-4 and its interaction with sitagliptin and inhibitor diprotin-A publication-title: Cell Biochemistry and Biophysics contributor: fullname: Agoramoorthy – volume: 19 start-page: 2883 year: 2018 ident: b0070 article-title: Bioactive peptides from germinated soybean with anti-diabetic potential by inhibition of dipeptidyl peptidase-IV, α-amylase, and α-glucosidase enzymes publication-title: International Journal of Molecular Sciences contributor: fullname: Martínez-Villaluenga – volume: 134 start-page: 797 year: 2012 end-page: 802 ident: b0075 article-title: Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran publication-title: Food Chemistry contributor: fullname: Mukaihara – volume: 57 start-page: 4552 year: 2009 end-page: 4558 ident: b0130 article-title: Composition, secondary structure, and self-assembly of oat protein isolate publication-title: Journal of Agricultural and Food Chemistry contributor: fullname: Huang – volume: 54 start-page: 863 year: 2015 end-page: 880 ident: b0220 article-title: Food protein-derived bioactive peptides in management of type 2 diabetes publication-title: European Journal of Nutrition contributor: fullname: Anand – volume: 35 start-page: 928 year: 2018 end-page: 935 ident: b0255 article-title: Inhibitory effect of peptide fractions derivatives from chia (Salvia hispanica) hydrolysis against α-amylase and α-glucosidase enzymes publication-title: Nutricion Hospitalaria contributor: fullname: Betancur-Ancona – volume: 91 start-page: 370 year: 2018 end-page: 379 ident: b0090 article-title: Structural properties of bioactive peptides with α-glucosidase inhibitory activity publication-title: Chemical Biology and Drug Design contributor: fullname: Gaspar – volume: 63 start-page: 9543 year: 2015 end-page: 9549 ident: b0300 article-title: Dipeptidyl Peptidase IV Inhibitory Peptides Derived from Oat (Avena sativa L.), Buckwheat (Fagopyrum esculentum), and Highland Barley (Hordeum vulgare trifurcatum (L.) Trofim) Proteins publication-title: Journal of Agricultural and Food Chemistry contributor: fullname: Fan – volume: 27 start-page: 269 year: 2012 end-page: 273 ident: b0195 article-title: Type 2 diabetes mellitus: A review of current trends publication-title: Oman Medical Journal contributor: fullname: Olokoba – volume: 9 start-page: 1 year: 2020 end-page: 15 ident: b0290 article-title: Antioxidant, physicochemical, and cellular secretion of glucagon-like peptide-1 properties of oat bran protein hydrolysates publication-title: Antioxidants contributor: fullname: Tsopmo – volume: 135 start-page: 2078 year: 2012 end-page: 2085 ident: b0330 article-title: Antidiabetic activity peptides from albumin against α-glucosidase and α-amylase publication-title: Food Chemistry contributor: fullname: Chen – volume: 27 start-page: 160 year: 2016 end-page: 177 ident: b0215 article-title: Common bean (Phaseolus vulgaris L.) protein-derived peptides increased insulin secretion, inhibited lipid accumulation, increased glucose uptake and reduced the phosphatase and tensin homologue activation in vitro publication-title: Journal of Functional Foods contributor: fullname: Amaya-Llano – volume: 190 start-page: 331 year: 2016 end-page: 337 ident: b0165 article-title: Enzyme-assisted extraction and identification of antioxidative and a-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto) publication-title: Food Chemistry contributor: fullname: Gan – volume: 76 start-page: 839 year: 2015 end-page: 851 ident: b0205 article-title: Hard-to-cook bean (Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress publication-title: Food Research International contributor: fullname: Amaya-Llano – volume: 47 start-page: 171 year: 2008 end-page: 182 ident: b0150 article-title: Bioactive peptides and proteins from foods: Indication for health effects publication-title: European Journal of Nutrition contributor: fullname: Schrezenmeir – volume: 54 start-page: 2021 year: 2019 end-page: 2034 ident: b0020 article-title: Inhibition of the in vitro activities of α-amylase, α-glucosidase and pancreatic lipase by yellow field pea (Pisum sativum L.) protein hydrolysates publication-title: International Journal of Food Science and Technology contributor: fullname: Aluko – volume: 11 start-page: 235 year: 2014 end-page: 242 ident: b0085 article-title: Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats publication-title: Journal of Functional Foods contributor: fullname: Hsu – volume: 14 start-page: 343 year: 2020 end-page: 352 ident: b0315 article-title: Effect of enzymatic hydrolysis using endo- and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates publication-title: Journal of Food Measurement and Characterization contributor: fullname: Almutaimi – volume: 141 start-page: 2170 year: 2013 end-page: 2176 ident: b0135 article-title: The α-amylase and α-glucosidase inhibitory effects of Irish seaweed extracts publication-title: Food Chemistry contributor: fullname: Paul Ross – volume: 41 start-page: 242 year: 2015 end-page: 251 ident: b0100 article-title: Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico publication-title: BioFactors contributor: fullname: Weng – volume: 1 start-page: 239 year: 1978 end-page: 260 ident: b0230 article-title: Effect of Several Experimental Parameters on Combination of Red Kidney Bean (Phaseolus Vulgaris) α -amylase inhibitor with porcine pancreatic α -amylase publication-title: Journal of Food Biochemistry contributor: fullname: Whitaker – volume: 165 start-page: 2143 year: 2020 end-page: 2196 ident: b0260 article-title: Use of Alcalase in the production of bioactive peptides: A review publication-title: International Journal of Biological Macromolecules contributor: fullname: Fernandez-Lafuente – volume: 15 start-page: 107 year: 2006 end-page: 118 ident: b0115 article-title: Evaluation of clonal herbs of Lamiaceae species for management of diabetes and hypertension publication-title: Asia Pacific Journal of Clinical Nutrition contributor: fullname: Shetty – volume: 43 start-page: 1 year: 2019 end-page: 12 ident: b0190 article-title: Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins publication-title: Journal of Food Biochemistry contributor: fullname: FitzGerald – volume: 371 start-page: 277 year: 1999 end-page: 283 ident: b0110 article-title: Comparative study of the inhibition of α-glucosidase, α-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose publication-title: Archives of Biochemistry and Biophysics contributor: fullname: Park – volume: 51 start-page: 1903 year: 2011 end-page: 1914 ident: b0320 article-title: Genotype × location interaction patterns and testing strategies for oat in the Canadian prairies publication-title: Crop Science contributor: fullname: Ames – volume: 1 start-page: 239 issue: 3 year: 1978 ident: 10.1016/j.jff.2021.104829_b0230 article-title: Effect of Several Experimental Parameters on Combination of Red Kidney Bean (Phaseolus Vulgaris) α -amylase inhibitor with porcine pancreatic α -amylase publication-title: Journal of Food Biochemistry doi: 10.1111/j.1745-4514.1978.tb00184.x contributor: fullname: Powers – volume: 13 start-page: 147 issue: 4 year: 2014 ident: 10.1016/j.jff.2021.104829_b0210 article-title: Proteins and bioactive peptides publication-title: Nutrafoods doi: 10.1007/s13749-014-0052-z contributor: fullname: Oseguera-Toledo – volume: 54 start-page: 863 issue: 6 year: 2015 ident: 10.1016/j.jff.2021.104829_b0220 article-title: Food protein-derived bioactive peptides in management of type 2 diabetes publication-title: European Journal of Nutrition doi: 10.1007/s00394-015-0974-2 contributor: fullname: Patil – volume: 42 start-page: 12 year: 2018 ident: 10.1016/j.jff.2021.104829_b0305 article-title: Oat globulin peptides regulate antidiabetic drug targets and glucose transporters in Caco-2 cells publication-title: Journal of Functional Foods doi: 10.1016/j.jff.2017.12.061 contributor: fullname: Wang – volume: 70 start-page: 907 issue: 2 year: 2014 ident: 10.1016/j.jff.2021.104829_b0035 article-title: Understanding the molecular dynamics of type-2 diabetes drug target DPP-4 and its interaction with sitagliptin and inhibitor diprotin-A publication-title: Cell Biochemistry and Biophysics doi: 10.1007/s12013-014-9998-0 contributor: fullname: Chakraborty – volume: 27 start-page: 269 year: 2012 ident: 10.1016/j.jff.2021.104829_b0195 article-title: Type 2 diabetes mellitus: A review of current trends publication-title: Oman Medical Journal doi: 10.5001/omj.2012.68 contributor: fullname: Olokoba – volume: 91 start-page: 370 issue: 2 year: 2018 ident: 10.1016/j.jff.2021.104829_b0090 article-title: Structural properties of bioactive peptides with α-glucosidase inhibitory activity publication-title: Chemical Biology and Drug Design doi: 10.1111/cbdd.13105 contributor: fullname: Ibrahim – volume: 37 start-page: 422 issue: 4 year: 1984 ident: 10.1016/j.jff.2021.104829_b0270 article-title: Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria publication-title: The Journal of Antibiotics doi: 10.7164/antibiotics.37.422 contributor: fullname: Umezawa – volume: 43 start-page: 1 issue: 1 year: 2019 ident: 10.1016/j.jff.2021.104829_b0190 article-title: Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins publication-title: Journal of Food Biochemistry doi: 10.1111/jfbc.12451 contributor: fullname: Nongonierma – volume: 2016 start-page: 1 year: 2016 ident: 10.1016/j.jff.2021.104829_b0280 article-title: Pepsin digested oat bran proteins: Separation, antioxidant activity, and identification of new peptides publication-title: Journal of Chemistry doi: 10.1155/2016/8216378 contributor: fullname: Vanvi – volume: 14 start-page: 163 issue: 4 year: 2016 ident: 10.1016/j.jff.2021.104829_b0015 article-title: In vitro antioxidant and α-amylase inhibitory properties of watermelon seed protein hydrolysates publication-title: Environmental and Experimental Biology doi: 10.22364/eeb.14.23 contributor: fullname: Arise – ident: 10.1016/j.jff.2021.104829_b0125 – volume: 9 start-page: 1 issue: 6 year: 2020 ident: 10.1016/j.jff.2021.104829_b0290 article-title: Antioxidant, physicochemical, and cellular secretion of glucagon-like peptide-1 properties of oat bran protein hydrolysates publication-title: Antioxidants doi: 10.3390/antiox9060557 contributor: fullname: Walters – volume: 135 start-page: 2078 issue: 3 year: 2012 ident: 10.1016/j.jff.2021.104829_b0330 article-title: Antidiabetic activity peptides from albumin against α-glucosidase and α-amylase publication-title: Food Chemistry doi: 10.1016/j.foodchem.2012.06.088 contributor: fullname: Yu – ident: 10.1016/j.jff.2021.104829_b0160 doi: 10.1016/j.bbrc.2013.03.010 – volume: 165 start-page: 2143 year: 2020 ident: 10.1016/j.jff.2021.104829_b0260 article-title: Use of Alcalase in the production of bioactive peptides: A review publication-title: International Journal of Biological Macromolecules doi: 10.1016/j.ijbiomac.2020.10.060 contributor: fullname: Tacias-Pascacio – ident: 10.1016/j.jff.2021.104829_b0180 doi: 10.1039/c3fo60262a – volume: 19 start-page: 2883 issue: 10 year: 2018 ident: 10.1016/j.jff.2021.104829_b0070 article-title: Bioactive peptides from germinated soybean with anti-diabetic potential by inhibition of dipeptidyl peptidase-IV, α-amylase, and α-glucosidase enzymes publication-title: International Journal of Molecular Sciences doi: 10.3390/ijms19102883 contributor: fullname: González-Montoya – volume: 54 start-page: 2021 issue: 6 year: 2019 ident: 10.1016/j.jff.2021.104829_b0020 article-title: Inhibition of the in vitro activities of α-amylase, α-glucosidase and pancreatic lipase by yellow field pea (Pisum sativum L.) protein hydrolysates publication-title: International Journal of Food Science and Technology doi: 10.1111/ijfs.14087 contributor: fullname: Awosika – volume: 55 start-page: 418 year: 2014 ident: 10.1016/j.jff.2021.104829_b0170 article-title: Effects of partial hydrolysis on structure and gelling properties of oat globular proteins publication-title: Food Research International doi: 10.1016/j.foodres.2013.11.038 contributor: fullname: Nieto-Nieto – ident: 10.1016/j.jff.2021.104829_b0055 doi: 10.1016/j.foodchem.2018.11.110 – volume: 57 start-page: 9234 issue: 19 year: 2009 ident: 10.1016/j.jff.2021.104829_b0040 article-title: Angiotensin-I Converting Enzyme Inhibitory Activity of Hydrolysates from Oat (Avena sativa) Proteins by In Silico and In Vitro Analyses publication-title: Journal of Agricultural and Food Chemistry doi: 10.1021/jf9018245 contributor: fullname: Cheung – ident: 10.1016/j.jff.2021.104829_b0120 doi: 10.1039/C6FO01411A – ident: 10.1016/j.jff.2021.104829_b0295 doi: 10.1021/acs.jafc.5b04016 – volume: 371 start-page: 277 issue: 2 year: 1999 ident: 10.1016/j.jff.2021.104829_b0110 article-title: Comparative study of the inhibition of α-glucosidase, α-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose publication-title: Archives of Biochemistry and Biophysics doi: 10.1006/abbi.1999.1423 contributor: fullname: Kim – ident: 10.1016/j.jff.2021.104829_b0050 doi: 10.1039/9781847557698 – volume: 68 start-page: 1858 issue: 9 year: 2014 ident: 10.1016/j.jff.2021.104829_b0060 article-title: Importance of the B Ring and Its Substitution on the α-Glucosidase Inhibitory Activity of Baicalein, 5,6,7-Trihydroxyflavone Hong GAO & Jun KAWABATA publication-title: Bioscience, Biotechnology, and Biochemistry doi: 10.1271/bbb.68.1858 contributor: fullname: Gao – volume: 47 start-page: 171 issue: 4 year: 2008 ident: 10.1016/j.jff.2021.104829_b0150 article-title: Bioactive peptides and proteins from foods: Indication for health effects publication-title: European Journal of Nutrition doi: 10.1007/s00394-008-0710-2 contributor: fullname: Möller – ident: 10.1016/j.jff.2021.104829_b0225 doi: 10.1094/9781891127649.008 – volume: 41 start-page: 242 issue: 4 year: 2015 ident: 10.1016/j.jff.2021.104829_b0100 article-title: Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico publication-title: BioFactors doi: 10.1002/biof.1219 contributor: fullname: Jhong – volume: 2013 year: 2013 ident: 10.1016/j.jff.2021.104829_b0240 article-title: Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis publication-title: International Journal of Food Science contributor: fullname: Rubi – volume: 61 start-page: 1138 issue: 7 year: 1997 ident: 10.1016/j.jff.2021.104829_b0175 article-title: Isolation and Activity of N-p-Coumaroyltyramine, an α-Glucosidase Inhibitor in Welsh Onion (Allium fistulosum) publication-title: Bioscience, Biotechnology, and Biochemistry doi: 10.1271/bbb.61.1138 contributor: fullname: Nishioka – volume: 42 start-page: 1 issue: 3 year: 2018 ident: 10.1016/j.jff.2021.104829_b0310 article-title: Evaluation of the antidiabetic activity of hydrolyzed peptides derived from Juglans mandshurica Maxim. fruits in insulin-resistant HepG2 cells and type 2 diabetic mice publication-title: Journal of Food Biochemistry doi: 10.1111/jfbc.12518 contributor: fullname: Wang – volume: 141 start-page: 2170 issue: 3 year: 2013 ident: 10.1016/j.jff.2021.104829_b0135 article-title: The α-amylase and α-glucosidase inhibitory effects of Irish seaweed extracts publication-title: Food Chemistry doi: 10.1016/j.foodchem.2013.04.123 contributor: fullname: Lordan – volume: 54 start-page: 259 issue: 3–4 year: 1999 ident: 10.1016/j.jff.2021.104829_b0140 article-title: Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate publication-title: Zeitschrift Fur Naturforschung - Section C Journal of Biosciences doi: 10.1515/znc-1999-3-417 contributor: fullname: Matsui – ident: 10.1016/j.jff.2021.104829_b0185 doi: 10.1016/j.foodchem.2013.08.097 – volume: 66 start-page: 4872 issue: 19 year: 2018 ident: 10.1016/j.jff.2021.104829_b0005 article-title: Identification of Bioactive Peptides with α-Amylase Inhibitory Potential from Enzymatic Protein Hydrolysates of Red Seaweed (Porphyra spp) [Research-article] publication-title: Journal of Agricultural and Food Chemistry doi: 10.1021/acs.jafc.8b00960 contributor: fullname: Admassu – volume: 57 start-page: 4552 issue: 11 year: 2009 ident: 10.1016/j.jff.2021.104829_b0130 article-title: Composition, secondary structure, and self-assembly of oat protein isolate publication-title: Journal of Agricultural and Food Chemistry doi: 10.1021/jf900135e contributor: fullname: Liu – volume: 194 start-page: 577 year: 2016 ident: 10.1016/j.jff.2021.104829_b0325 article-title: In vitro inhibition of platelet aggregation by peptides derived from oat (Avena sativa L.), highland barley (Hordeum vulgare Linn. var. nudum Hook. f.), and buckwheat (Fagopyrum esculentum Moench) proteins publication-title: Food Chemistry doi: 10.1016/j.foodchem.2015.08.058 contributor: fullname: Yu – ident: 10.1016/j.jff.2021.104829_b0095 – volume: 15 start-page: 107 issue: 1 year: 2006 ident: 10.1016/j.jff.2021.104829_b0115 article-title: Evaluation of clonal herbs of Lamiaceae species for management of diabetes and hypertension publication-title: Asia Pacific Journal of Clinical Nutrition contributor: fullname: Kwon – volume: 44 start-page: 1752 issue: 8 year: 2011 ident: 10.1016/j.jff.2021.104829_b0200 article-title: Antioxidant activity of amaranth protein or their hydrolysates under simulated gastrointestinal digestion publication-title: LWT - Food Science and Technology doi: 10.1016/j.lwt.2011.04.002 contributor: fullname: Orsini Delgado – ident: 10.1016/j.jff.2021.104829_b0030 doi: 10.1093/jxb/34.10.1320 – volume: 26 start-page: 439 year: 2016 ident: 10.1016/j.jff.2021.104829_b0235 article-title: Identification and characterization of two novel α-glucosidase inhibitory oligopeptides from hemp (Cannabis sativa L.) seed protein publication-title: Journal of Functional Foods doi: 10.1016/j.jff.2016.07.024 contributor: fullname: Ren – volume: 15 start-page: 141 year: 2012 ident: 10.1016/j.jff.2021.104829_b0045 article-title: α-amylase inhibitors: A review of raw material and isolated compounds from plant source publication-title: Journal of Pharmacy and Pharmaceutical Sciences doi: 10.18433/J35S3K contributor: fullname: de Sales – volume: 16 start-page: 117 issue: 2 year: 2019 ident: 10.1016/j.jff.2021.104829_b0025 article-title: An Insight of Alpha-amylase Inhibitors as a Valuable Tool in the Management of Type 2 Diabetes Mellitus publication-title: Current Diabetes Reviews doi: 10.2174/1573399815666190618093315 contributor: fullname: Bashary – volume: 37 start-page: 1944 issue: 11 year: 2020 ident: 10.1016/j.jff.2021.104829_b0080 article-title: Improving understanding of type 2 diabetes remission: research recommendations from Diabetes UK’s 2019 remission workshop publication-title: Diabetic Medicine doi: 10.1111/dme.14358 contributor: fullname: Hopkins – volume: 134 start-page: 797 issue: 2 year: 2012 ident: 10.1016/j.jff.2021.104829_b0075 article-title: Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran publication-title: Food Chemistry doi: 10.1016/j.foodchem.2012.02.183 contributor: fullname: Hatanaka – start-page: 15 year: 2017 ident: 10.1016/j.jff.2021.104829_b0265 article-title: Technology of main ingredients—Water and flours contributor: fullname: Tiefenbacher – volume: 35 start-page: 928 issue: 4 year: 2018 ident: 10.1016/j.jff.2021.104829_b0255 article-title: Inhibitory effect of peptide fractions derivatives from chia (Salvia hispanica) hydrolysis against α-amylase and α-glucosidase enzymes publication-title: Nutricion Hospitalaria doi: 10.20960/nh.1713 contributor: fullname: Sosa Crespo – volume: 136 start-page: 758 issue: 2 year: 2013 ident: 10.1016/j.jff.2021.104829_b0285 article-title: In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins publication-title: Food Chemistry doi: 10.1016/j.foodchem.2012.08.032 contributor: fullname: Velarde-Salcedo – volume: 190 start-page: 331 year: 2016 ident: 10.1016/j.jff.2021.104829_b0165 article-title: Enzyme-assisted extraction and identification of antioxidative and a-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto) publication-title: Food Chemistry doi: 10.1016/j.foodchem.2015.05.120 contributor: fullname: Ngoh – volume: 63 start-page: 9543 issue: 43 year: 2015 ident: 10.1016/j.jff.2021.104829_b0300 article-title: Dipeptidyl Peptidase IV Inhibitory Peptides Derived from Oat (Avena sativa L.), Buckwheat (Fagopyrum esculentum), and Highland Barley (Hordeum vulgare trifurcatum (L.) Trofim) Proteins publication-title: Journal of Agricultural and Food Chemistry doi: 10.1021/acs.jafc.5b04016 contributor: fullname: Wang – volume: 21 start-page: 517 issue: 4 year: 2007 ident: 10.1016/j.jff.2021.104829_b0010 article-title: DPP-4 inhibitors publication-title: Best Practice and Research in Clinical Endocrinology and Metabolism doi: 10.1016/j.beem.2007.07.005 contributor: fullname: Ahrén – volume: 27 start-page: 160 year: 2016 ident: 10.1016/j.jff.2021.104829_b0215 article-title: Common bean (Phaseolus vulgaris L.) protein-derived peptides increased insulin secretion, inhibited lipid accumulation, increased glucose uptake and reduced the phosphatase and tensin homologue activation in vitro publication-title: Journal of Functional Foods doi: 10.1016/j.jff.2016.09.001 contributor: fullname: Oseguera Toledo – volume: 75 start-page: 1472 issue: 8 year: 2011 ident: 10.1016/j.jff.2021.104829_b0155 article-title: Protein Tyrosine Phosphatase 1B and α-Glucosidase Inhibitory Phlorotannins from Edible Brown Algae, Ecklonia stolonifera and Eiseniaï¿¿bicyclis publication-title: Biotechnology and Biochemistry doi: 10.1271/bbb.110137 contributor: fullname: Moon – volume: 19 issue: 1 year: 2019 ident: 10.1016/j.jff.2021.104829_b0275 article-title: Patients’ perspective on self-management: Type 2 diabetes in daily life publication-title: BMC Health Services Research doi: 10.1186/s12913-019-4384-7 contributor: fullname: Van Smoorenburg – volume: 5 start-page: 2863 issue: 13 year: 2011 ident: 10.1016/j.jff.2021.104829_b0245 article-title: Inhibitory effects of five medicinal plants on rat alpha-glucosidase: Comparison with their effects on yeast alpha-glucosidase publication-title: Journal of Medicinal Plants Research contributor: fullname: Shai – volume: 15 start-page: 69 issue: 2 year: 2019 ident: 10.1016/j.jff.2021.104829_b0250 article-title: A review on microbial alkaline protease: An essential tool for various industrial approaches publication-title: Industrial Biotechnology doi: 10.1089/ind.2018.0032 contributor: fullname: Sharma – volume: 51 start-page: 1903 issue: 5 year: 2011 ident: 10.1016/j.jff.2021.104829_b0320 article-title: Genotype × location interaction patterns and testing strategies for oat in the Canadian prairies publication-title: Crop Science doi: 10.2135/cropsci2010.09.0548 contributor: fullname: Yan – volume: 20 start-page: 5978 issue: 23 year: 2019 ident: 10.1016/j.jff.2021.104829_b0145 article-title: BIOPEP-UWM database of bioactive peptides: Current opportunities publication-title: International Journal of Molecular Sciences doi: 10.3390/ijms20235978 contributor: fullname: Minkiewicz – start-page: 1 year: 2011 ident: 10.1016/j.jff.2021.104829_b0105 contributor: fullname: Kannan – volume: 11 start-page: 235 issue: C year: 2014 ident: 10.1016/j.jff.2021.104829_b0085 article-title: Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats publication-title: Journal of Functional Foods doi: 10.1016/j.jff.2014.09.010 contributor: fullname: Huang – volume: 4 start-page: 175 issue: 2 year: 2013 ident: 10.1016/j.jff.2021.104829_b0065 article-title: Adherence to therapies in patients with type 2 diabetes publication-title: Diabetes Therapy doi: 10.1007/s13300-013-0034-y contributor: fullname: García-Pérez – volume: 76 start-page: 839 year: 2015 ident: 10.1016/j.jff.2021.104829_b0205 article-title: Hard-to-cook bean (Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress publication-title: Food Research International doi: 10.1016/j.foodres.2015.07.046 contributor: fullname: Oseguera-Toledo – volume: 14 start-page: 343 issue: 1 year: 2020 ident: 10.1016/j.jff.2021.104829_b0315 article-title: Effect of enzymatic hydrolysis using endo- and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates publication-title: Journal of Food Measurement and Characterization doi: 10.1007/s11694-019-00296-0 contributor: fullname: Xu |
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•Oat protein treated by alcalase and flavourzyme is a good source of antidiabetic peptides.•Oat peptides can inhibit three of the main... The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the... |
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SubjectTerms | Antidiabetic peptides DPP-IV inhibition Oat protein Peptide sequencing Type 2 diabetes α-amylase inhibition |
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Title | Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein |
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