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Study On The Interaction Between Mung Bean Protein And Vitexin

Posted on:2022-10-18Degree:MasterType:Thesis
Country:ChinaCandidate:H GuoFull Text:PDF
GTID:2511306320470304Subject:Food processing and security
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Mung bean is a common legume grain crop with low price and rich nutrition.It has a variety of health care effects.The nutrition and health care effect of mung bean is closely related to its rich active components.Mung beans before eating need to carry on the processing,processing of mung bean components such as flavonoid composition,protein will have varying degrees of impact,to change their efficacy,for green beans in the processing medium yellow ketone components and protein interaction studies available information is limited,therefore,this paper obtained from mung bean yellow ketone,Continuous preparative chromatography was used to isolate and purify flavonoids with the strongest antioxidant activity,and their structures were identified.Then the interaction between the typical components of mung bean flavonoids and proteins in different proportions and different simulated processing temperatures was investigated,and the physicochemical and structural properties of the interaction products were analyzed.The specific conclusions are as follows:1.Structure identification of flavonoids in mung bean.The flavonoids of mung bean were classified by continuous preparative chromatography.Taking antioxidant capacity as an index,the antioxidant capacity of the 60% eluted components was the strongest,and the DPPH· scavenging capacity was 48.03%.ABTS+· scavenging capacity 57.53%;·OH scavenging capacity was 12.02%;The antioxidant activity of T-AOC was 207.64U/m L,which was significantly higher than that of other eluted components(p <0.05).According to the structure identification,the flavonoids with the strongest antioxidant activity in mung bean flavonoids are isovitexin,vitexin,eriodictyol-6-C-?-D-glucopyraoside,respectively.The content of vitexin is higher.2.Study on the interaction between vitexin at different concentrations and Mung bean protein.According to the physical and chemical properties after the interaction of vitexin-MBP with different concentrations,the solubility,foaming property,emulsification property and antioxidant activity of the vitexin-MBP complex were all improved.When the concentration of vitexin-MBP was 60(?mol/g),the concentrationof vitexin-MBP increased.The solubility of vitexin-MBP,DPPH·,ABTS+· and total antioxidant capacity of T-AOC were the highest,and were significantly higher than those of other interaction ratios(p <0.05).Fourier transform infrared spectroscopy(FIR)analysis showed that the interaction with vitexin changed the structure of MBP,the content of ?-helix and ?-fold decreased,and the structure of MBP expanded.The surface hydrophobicity of vitexin-MBP decreased with the increase of vitexin-concentration,which further explained the effect of interaction on protein structure.3.Study on the interaction between vitexin and MBP at different temperatures.The results showed that the physical and chemical properties of vitexin-MBP were different at different temperatures.The emulsification,foaming and foam stability of vitexin-MBP were the best when the vitexin-MBP interacted at 90?.Fourier transform infrared spectroscopy(FIR)analysis showed that the structure of the protein was expanded when the temperature increased,and the interaction between vitexin and MBP was mainly hydrophobic by fluorescence spectrum analysis.Based on the above research results,it is concluded that both concentration and temperature can affect the interaction between vitexin-MBP,thus affecting the physicochemical properties and structure of vitexin-MBP molecule.In practical production and application,the interaction product of vitexin and MBP with the concentration of 60?mol/g has the best functional activity.In order to ensure the sample ripening and antioxidant activity,90? was the optimal processing temperature.
Keywords/Search Tags:Flavonoids, Mung bean protein, Antioxidant, Functional properties, Structure
PDF Full Text Request
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