Wedad Q Al-Bukhaiti, Sam Al-Dalali, Hanxiang Li, Liyuan Yao, Sherif M Abed, Liyun Zhao, Sheng-Xiang Qiu
{"title":"花生蛋白酶解新型抗糖尿病肽的鉴定与体外表征","authors":"Wedad Q Al-Bukhaiti, Sam Al-Dalali, Hanxiang Li, Liyuan Yao, Sherif M Abed, Liyun Zhao, Sheng-Xiang Qiu","doi":"10.1007/s11130-023-01118-x","DOIUrl":null,"url":null,"abstract":"<p><p>Bioactive peptides derived from proteins found in various foods provide significant health benefits, including regulating blood sugar levels by inhibiting carbohydrate-hydrolyzing enzymes. Hydrolysates of peanut protein were prepared using alcalase (AH) or trypsin (TH) to generate antidiabetic peptides with high activity against α-amylase (IC<sub>50</sub> of 6.46 and 5.71 mg/mL) and α-glucosidase (IC<sub>50</sub> of 6.30 and 5.57 mg/mL), as well as antiradical activity to scavenge DPPH<sup>•</sup> (IC<sub>50</sub> of 4.18 and 3.12 mg/mL) and ABTS<sup>•+</sup> (IC<sub>50</sub> of 2.87 and 2.56 mg/mL), respectively. The bioactivities of hydrolysates were greatest in the ultrafiltration-generated F3 fraction (< 3 kDa). The most active fraction was TH-F3, which was purified by gel filtration chromatography to generate sub-fractions (SF). With IC<sub>50</sub> values of 1.05 and 0.69 mg/mL, the F3-SF8 fraction was the most effective at inhibiting the activity of α-amylase and α-glucosidase, respectively. This fraction was further purified using RP-HPLC to generate sub-subfractions (SSF), the most active of which were F3-SF8-SSF9 and SSF10. The peptide sequences F3-SF8-SSF9 and SSF10 were determined using LC-MS/MS. Two novel antidiabetic peptides with the potential to inhibit α-amylase and α-glucosidase were identified, with the sequences Asp-Trp-Arg (476.22 Da, IC<sub>50</sub> of 0.78, and 0.35 mg/mL) and Phe-Tyr (329.15 Da, IC<sub>50</sub> of 0.91, and 0.41 mg/mL). These results suggest that peptides derived from peanut protein are attractive natural ingredients for diabetes management applications.</p>","PeriodicalId":20092,"journal":{"name":"Plant Foods for Human Nutrition","volume":null,"pages":null},"PeriodicalIF":3.1000,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification and in vitro Characterization of Novel Antidiabetic Peptides Released Enzymatically from Peanut Protein.\",\"authors\":\"Wedad Q Al-Bukhaiti, Sam Al-Dalali, Hanxiang Li, Liyuan Yao, Sherif M Abed, Liyun Zhao, Sheng-Xiang Qiu\",\"doi\":\"10.1007/s11130-023-01118-x\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Bioactive peptides derived from proteins found in various foods provide significant health benefits, including regulating blood sugar levels by inhibiting carbohydrate-hydrolyzing enzymes. Hydrolysates of peanut protein were prepared using alcalase (AH) or trypsin (TH) to generate antidiabetic peptides with high activity against α-amylase (IC<sub>50</sub> of 6.46 and 5.71 mg/mL) and α-glucosidase (IC<sub>50</sub> of 6.30 and 5.57 mg/mL), as well as antiradical activity to scavenge DPPH<sup>•</sup> (IC<sub>50</sub> of 4.18 and 3.12 mg/mL) and ABTS<sup>•+</sup> (IC<sub>50</sub> of 2.87 and 2.56 mg/mL), respectively. The bioactivities of hydrolysates were greatest in the ultrafiltration-generated F3 fraction (< 3 kDa). The most active fraction was TH-F3, which was purified by gel filtration chromatography to generate sub-fractions (SF). With IC<sub>50</sub> values of 1.05 and 0.69 mg/mL, the F3-SF8 fraction was the most effective at inhibiting the activity of α-amylase and α-glucosidase, respectively. This fraction was further purified using RP-HPLC to generate sub-subfractions (SSF), the most active of which were F3-SF8-SSF9 and SSF10. The peptide sequences F3-SF8-SSF9 and SSF10 were determined using LC-MS/MS. Two novel antidiabetic peptides with the potential to inhibit α-amylase and α-glucosidase were identified, with the sequences Asp-Trp-Arg (476.22 Da, IC<sub>50</sub> of 0.78, and 0.35 mg/mL) and Phe-Tyr (329.15 Da, IC<sub>50</sub> of 0.91, and 0.41 mg/mL). These results suggest that peptides derived from peanut protein are attractive natural ingredients for diabetes management applications.</p>\",\"PeriodicalId\":20092,\"journal\":{\"name\":\"Plant Foods for Human Nutrition\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.1000,\"publicationDate\":\"2024-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Foods for Human Nutrition\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1007/s11130-023-01118-x\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/11/23 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Foods for Human Nutrition","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1007/s11130-023-01118-x","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/11/23 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Identification and in vitro Characterization of Novel Antidiabetic Peptides Released Enzymatically from Peanut Protein.
Bioactive peptides derived from proteins found in various foods provide significant health benefits, including regulating blood sugar levels by inhibiting carbohydrate-hydrolyzing enzymes. Hydrolysates of peanut protein were prepared using alcalase (AH) or trypsin (TH) to generate antidiabetic peptides with high activity against α-amylase (IC50 of 6.46 and 5.71 mg/mL) and α-glucosidase (IC50 of 6.30 and 5.57 mg/mL), as well as antiradical activity to scavenge DPPH• (IC50 of 4.18 and 3.12 mg/mL) and ABTS•+ (IC50 of 2.87 and 2.56 mg/mL), respectively. The bioactivities of hydrolysates were greatest in the ultrafiltration-generated F3 fraction (< 3 kDa). The most active fraction was TH-F3, which was purified by gel filtration chromatography to generate sub-fractions (SF). With IC50 values of 1.05 and 0.69 mg/mL, the F3-SF8 fraction was the most effective at inhibiting the activity of α-amylase and α-glucosidase, respectively. This fraction was further purified using RP-HPLC to generate sub-subfractions (SSF), the most active of which were F3-SF8-SSF9 and SSF10. The peptide sequences F3-SF8-SSF9 and SSF10 were determined using LC-MS/MS. Two novel antidiabetic peptides with the potential to inhibit α-amylase and α-glucosidase were identified, with the sequences Asp-Trp-Arg (476.22 Da, IC50 of 0.78, and 0.35 mg/mL) and Phe-Tyr (329.15 Da, IC50 of 0.91, and 0.41 mg/mL). These results suggest that peptides derived from peanut protein are attractive natural ingredients for diabetes management applications.
期刊介绍:
Plant Foods for Human Nutrition (previously Qualitas Plantarum) is an international journal that publishes reports of original research and critical reviews concerned with the improvement and evaluation of the nutritional quality of plant foods for humans, as they are influenced by:
- Biotechnology (all fields, including molecular biology and genetic engineering)
- Food science and technology
- Functional, nutraceutical or pharma foods
- Other nutrients and non-nutrients inherent in plant foods