食品科学 ›› 2023, Vol. 44 ›› Issue (4): 194-199.doi: 10.7506/spkx1002-6630-20220624-278

• 生物工程 • 上一篇    下一篇

面筋蛋白咸味肽的分离纯化及结构鉴定

温青玉,张雨,李天齐,张康逸   

  1. (1.河南省农业科学院农副产品加工研究中心,河南省全谷物小麦制品加工国际联合实验室,河南省全谷物鲜食加工工程技术研究中心,河南 郑州 450002;2.河南省安康食品科技研究院,河南 郑州 450047;3.河南省安康未来食品科技有限公司,河南 郑州 450066)
  • 发布日期:2023-03-01
  • 基金资助:
    河南省重大公益专项(201300110300);河南省科技攻关项目(222102110256); 河南省农业科学院优秀青年科技基金项目(2022YQ30);河南省农业科学院科技创新团队项目(2022TD24)

Isolation, Purification and Structure Identification of Salty Peptides from Wheat Gluten

WEN Qingyu, ZHANG Yu, Li Tianqi, ZHANG Kangyi   

  1. (1. Center of Agricultural Products Processing, Henan Academy of Agricultural Sciences, Henan Province International Joint Laboratory for Whole Grain Wheat Processing, Henan Province Whole Grain Fresh, Food Processing Engineering Technology Research Center, Zhengzhou 450002, China; 2. Henan Ankang Food Science and Technology Research Institute, Zhengzhou 450047, China; 3. Henan Ankang Future Food Technology Co. Ltd., Zhengzhou 450066, China)
  • Published:2023-03-01

摘要: 为了明确面筋蛋白酶解液中的咸味肽序列,对面筋蛋白咸味酶解物进行了分离纯化和结构鉴定。对酶解物脱盐处理后进行分离纯化。经过分级超滤,选择咸味最高、分子质量1 000 Da以下的组分进行葡聚糖凝胶Sephadex G-15过滤层析,结合感官评定结果筛选出咸味最强的组分,并利用液相色谱-串联质谱鉴定其氨基酸序列。最终得到面筋蛋白中咸味肽氨基酸序列为PFGQQ、PFSPQ、QPFP、PDFP、FDDP,分子质量分别为576.28、575.28、488.25、475.22、493.21 Da。本研究为面筋蛋白咸味肽的开发提供了一定理论依据。

关键词: 面筋蛋白;咸味肽;纯化;鉴定;氨基酸序列

Abstract: The salty enzymatic hydrolysate of wheat gluten was desalted and fractionated into four fractions (F1–F5). F4, which had the highest salty taste and proportion of peptides with molecular mass below 1 000 Da among these fractions, was further fractionated by Sephadex G-15 gel filtration chromatography into five subfractions (P1–P5). Among these subfractions, P2 was found to have the highest content of salty peptides and the strongest salty taste. By liquid chromatography tandem mass spectrometry (LC-MS/MS), the amino acid sequences of P2 were identified as PFGQQ, PFSPQ, QPFP, PDFP and FDDP, with molecular masses of 576.28, 575.28, 488.25, 475.22 and 493.21 Da, respectively. The results provide a theoretical basis for the development of salty peptides from gluten protein.

Key words: gluten proteins; salty peptides; purification; identification; amino acid sequences

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