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Studies on Functional Properties of 11S and 7S Globulin in Soybean and Interaction between Protein and Starch

Author: ChenXueLing
Tutor: PanSiZuo
School: Huazhong Agricultural University
Course: Of Food Science
Keywords: 11S globulin 7S globulin Modified Features Conformation Starch Interactions
CLC: TS201.2
Type: Master's thesis
Year: 2005
Downloads: 617
Quote: 5
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Abstract


The high nutritional value of soy protein, rich in natural resources, low cost of raw materials, food and hobbies, workability, and other functional properties associated. 11S and 7S globulin is its main component, and play an important role in the functional properties of soy protein. In recent years, the functional properties of 11S and 7S globulin rarely reported, 11S or 7S globulin and starch composite system has not been reported in detail. This article is extracted from soybean, isolation and identification of the 11S and 7S globulin with higher purity, and evaluation of the functional properties of its modified, and the preliminary study and starch composite after the rheological properties of the system, thermal denaturation and textural characteristics. The main findings are as follows: 1,11 S and 7S globulin extraction, separation, purification and identification of comparing the three extraction methods based on the target 11S and 7S globulin relative purity determined Thanh law as the experimental method. On the basis of law in Thanh, the experimental comparison of the extraction effect of the three kinds of extraction buffer, the results show that using Tris-HCl (pH 8.0, 0.03mol / L mercaptoethanol) buffer 7S and 11S globulin in the highest extraction rate. 11S and 7S globulin purified using ammonium sulfate precipitation and gel filtration, 11S and 7S globulin purified effect, can be seen through the gel filtration pattern of the levels of the purified protein. SDS-PAGE gel filtration spectrum peaks unity and the Kjeldahl method identified protein purity. The results showed that the SDS-PAGE for and reported in the literature are consistent, gel filtration spectra showed a single peak, and the protein content of up to 95%, has reached the research required purity. 2,11 S and 7S globulin conformational characterization using Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD), atomic force microscopy (AFM) and differential scanning calorimetry (DSC) of 11S and 7S globulin conformations preliminary characterization. Can be seen from the Fourier transform infrared spectra of 11S and 7S globulin mainly α-helical structure, in line with the conclusion of circular dichroism Figure. The atomic force microscope neutral solution 7S and 11S globulin showed spherical diameter of approximately 56nm and 105nm. DSC results showed that 7S and 11S globulin denaturation endothermic peak of 58.9 ℃ and 60.6 ℃, respectively, this process may be a protein spatial structure was destroyed in the process according to the principle of protein thermal denaturation.

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CLC: > Industrial Technology > Light industry,handicrafts > Food Industry > General issues > Basic science > Food Chemistry
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