Raman Spectral Analysis of the Structure of Soybean Meal Protein from Aqueous Enzymatic Extraction of Soybean Oil as Affected by Ultrafine Grinding at Low Temperature

doi:10.7506/spkx1002-6630-20180109-104

Abstract

Abstract: The purpose of the present study was to determine the effect of ultrafine grinding at low temperature on the structure of soybean meal protein from aqueous enzymatic oil extraction. Soybean meal was oven dried and ground into ultrafine powders with different particle sizes (100, 200 and 300 mesh) at room temperature or low temperature. Raman spectroscopy was used to analyze the structural changes of soybean meal protein. The results showed that ultrafine grinding at low temperature increased the contents of α-helix and β-sheet and decreased the content of β-turn. Trp and tyr and aliphatic amino acid residues were exposed on the protein surface. Ultrafine grinding at low temperature significantly increased the disulfide bond mode t-g-t. The disordered structure of soybean meal protein turned into an ordered one after ultrafine grinding at low temperature.

Key words: aqueous enzymatic extraction of soybean oil, ultrafine grinding at low temperature, soybean meal protein, Raman spectroscopy

CLC Number:

TS201.2

WU Changling, XUN Chongrong, LIU Baohua, WANG Zhongjiang, TENG Fei, JIANG Lianzhou, LI Yang. Raman Spectral Analysis of the Structure of Soybean Meal Protein from Aqueous Enzymatic Extraction of Soybean Oil as Affected by Ultrafine Grinding at Low Temperature[J]. FOOD SCIENCE, 2019, 40(7): 33-39.

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Raman Spectral Analysis of the Structure of Soybean Meal Protein from Aqueous Enzymatic Extraction of Soybean Oil as Affected by Ultrafine Grinding at Low Temperature

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