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                  • EI
                  • Scopus
                  • 食品科學與工程領域高質量科技期刊分級目錄第一方陣T1
                  • DOAJ
                  • EBSCO
                  • 北大核心期刊
                  • 中國核心學術期刊RCCSE
                  • JST China
                  • FSTA
                  • 中國精品科技期刊
                  • 中國農業核心期刊
                  • CA
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                  • 中國科技核心期刊CSTPCD
                  • 中國生物醫學SinoMed
                  中國精品科技期刊2020
                  昝麗霞,王威威,張文夷,等. 超濾親和結合液相色譜-質譜聯用和分子對接技術篩選茶葉中α-葡萄糖苷酶抑制肽[J]. 食品工業科技,2023,44(18):300?306. doi: 10.13386/j.issn1002-0306.2023030066.
                  引用本文: 昝麗霞,王威威,張文夷,等. 超濾親和結合液相色譜-質譜聯用和分子對接技術篩選茶葉中α-葡萄糖苷酶抑制肽[J]. 食品工業科技,2023,44(18):300?306. doi: 10.13386/j.issn1002-0306.2023030066.
                  ZAN Lixia, WANG Weiwei, ZHANG Wenyi, et al. Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology[J]. Science and Technology of Food Industry, 2023, 44(18): 300?306. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023030066.
                  Citation: ZAN Lixia, WANG Weiwei, ZHANG Wenyi, et al. Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology[J]. Science and Technology of Food Industry, 2023, 44(18): 300?306. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023030066.

                  超濾親和結合液相色譜-質譜聯用和分子對接技術篩選茶葉中α-葡萄糖苷酶抑制肽

                  Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology

                  • 摘要: 目的:篩選茶葉中具有抑制α-葡萄糖苷酶活性的肽段。方法:采用響應面法優化茶葉酶解產物制備工藝,超濾親和法分離與α-葡萄糖苷酶結合的茶多肽,液相色譜-質譜聯用對分離肽段進行序列測定,生物信息學方法進行虛擬篩選。結果:茶葉酶解產物最佳制備工藝為堿性蛋白酶酶解溫度50 ℃,酶解時間3 h,液料比10:1 (mL/g),對α-葡萄糖苷酶抑制率為57.29%,從中鑒定出624條肽段,篩選出一條四肽LIGF具有α-葡萄糖苷酶抑制活性,在 5 mg/mL的濃度下對α-葡萄糖苷酶的最大抑制率為88.13%,IC50值為1.22 mg/mL。分子對接顯示,LIGF與α-葡萄糖苷酶能形成5個氫鍵,結合能為?3.51 kJ,具有高的親和力、穩定性以及與α-葡萄糖苷酶結合的能力。結論:LIGF具有成為II型糖尿病治療藥物的潛在價值。

                     

                    Abstract: Objective: To screen for tea peptides with inhibitory activity against α-glucosidase. Methods: The response surface method was used to optimize the preparation process of tea peptides. Affinity ultrafiltration was used to isolate tea peptides that bind with α-glucosidase, and liquid chromatography-mass spectrometry was used to determine the sequence of the isolated peptides. Virtual screening was performed using bioinformatics methods. Results: The optimal preparation process of tea leaf enzymatic hydrolysis products was alkaline protease hydrolysis temperature of 50 ℃, enzymatic hydrolysis time of 3 h, and a liquid-to-solid ratio of 10:1 (mL/g). The α-glucosidase inhibitory rate was 57.29%. From this, 624 peptide segments were identified, and LIGF was selected for its α-glucosidase inhibitory activity. At a concentration of 5 mg/mL, LIGF exhibited a maximum inhibition rate of 88.13% against α-glucosidase and an IC50 value of 1.22 mg/mL. Molecular docking showed that LIGF could form 5 hydrogen bonds with α-glucosidase, and the binding energy was ?3.51 kJ, indicating a high affinity, stability and ability to bind to α-glucosidase. Conclusion: LIGF had potential value as a therapeutic drug for type II diabetes.

                     

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