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Method for recovery of Kunitz and Bowman-Birk trypsin inhibitors from soybean whey

A technology of trypsin inhibition and soybean whey protein, which is applied in the direction of protease inhibitors, peptide preparation methods, chemical instruments and methods, etc., can solve complex and complicated processes and other problems, and achieve high purity, low equipment requirements, and simple operation Effect

Active Publication Date: 2015-04-15
JIANGNAN UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The existing technologies all adopt methods such as membrane separation or ion exchange chromatography, which generally have complex and complicated processes.

Method used

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  • Method for recovery of Kunitz and Bowman-Birk trypsin inhibitors from soybean whey
  • Method for recovery of Kunitz and Bowman-Birk trypsin inhibitors from soybean whey
  • Method for recovery of Kunitz and Bowman-Birk trypsin inhibitors from soybean whey

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0026] Adjust the soybean whey to pH 4.5, centrifuge (9500rpm, 30min) to remove the precipitate; adjust to pH 8.0 again, centrifuge (9500rpm, 30min), discard the precipitate, and collect the supernatant. Adjust the pH of the above supernatant to 4.5, measure 1L of the solution, add solid ammonium sulfate to 35% saturation according to the ammonium sulfate saturation table at 4-30°C, and centrifuge (9500rpm, 30min) to obtain KTI and BBI containing About 2.12g of crude protein was dissolved in 30mL of deionized water, dialyzed (molecular weight cut-off: 3500) for 36 hours to desalt, and the retentate was vacuum freeze-dried to prepare samples containing KTI and BBI inhibitors.

[0027]Accurately weigh 0.2g of the above primary separated KTI and BBI inhibitor samples and 0.2g of polyanionic polysaccharide powder respectively, add them into 100mL deionized water, stir until the two substances are completely dissolved, and prepare the mass concentration w / v of 0.2 % Homogeneous pro...

Embodiment 2

[0032] The soybean whey was adjusted to pH 4.5, centrifuged (9500rpm, 30min) to remove the precipitate; again adjusted to pH 8.5, centrifuged (9500rpm, 30min), the precipitate was discarded, and the supernatant was collected. Adjust the pH of the above supernatant to 4.7, measure 1.5L of the solution, add solid ammonium sulfate to 40% saturation according to the ammonium sulfate saturation table at 4-30°C, and centrifuge (9500rpm, 30min) to obtain KTI and About 3.35 g of crude BBI protein was dissolved in 40 mL of deionized water, dialyzed (molecular weight cut-off: 3500) for 48 hours, and vacuum freeze-dried to prepare the sample.

[0033] Accurately weigh 0.4g of the above primary separated KTI and BBI inhibitor samples and 0.4g of polyanionic polysaccharide powder respectively, add them to 100ml deionized water, stir until the two substances are completely dissolved, and prepare a homogeneous protein and polysaccharide with a mass concentration of 0.4%. solution. Both the ...

Embodiment 3

[0037] The soybean whey was adjusted to pH 4.8, centrifuged (9500rpm, 30min) to remove the precipitate; again adjusted to pH 9.0, centrifuged (9500rpm, 30min), the precipitate was discarded, and the supernatant was collected. Adjust the pH of the above supernatant to 4.8, measure 2L of the solution, add 30% saturated ammonium sulfate at 4-30°C according to the ammonium sulfate saturation table, and centrifuge to obtain about 0.356g of KTI and BBI protein crude products, add Dissolve in 10mL deionized water, dialyze (molecular weight cut-off: 3500) for 48 hours to desalt, and vacuum freeze-dry to prepare the sample.

[0038] Accurately weigh 0.15g of the above primary separated KTI and BBI inhibitor samples and 0.15g of polyanionic polysaccharide powder respectively, add to 100mL deionized water, stir until the two substances are completely dissolved, and prepare a homogeneous protein and polysaccharide with a mass concentration of 0.15% solution. Both the above soybean whey p...

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Abstract

Belonging to the field of agricultural product processing and by-product comprehensive utilization, the invention relates to a method for recovery of Kunitz and Bowman-Birk trypsin inhibitors from soybean whey. The method of the invention comprises the steps of: (1) pretreatment of soybean whey; (2) primary separation of whey soy protein; (3) complex coacervation of soybean whey protein and polyanionic polysaccharide; and (4) recovery of Kunitz and Bowman-Birk trypsin inhibitors. By subjecting the raw material to pretreatment, primary separation and complex coacervation, a final protein polysaccharide compound can be obtained, and after ultrafiltration for sugar removal, ultrafiltration for desalination, and twice centrifugation on the final protein polysaccharide compound, a protein solution containing purified Kunitz and Bowman-Birk trypsin inhibitors can be obtained, and through vacuum freeze drying of the protein solution, Kunitz and Bowman-Birk trypsin inhibitor high purity samples can be obtained. The method provided by the invention has the characteristics of comprehensive utilization of soybean whey, low equipment requirement, simple operation, and no environmental pollution. And the trypsin inhibitors have high recovery rate, high purity, and high protein activity.

Description

technical field [0001] The invention relates to a method for recovering soybean whey protein, specifically a method for recovering Kunitz and Bowman-Birk type trypsin inhibitors in soybean whey by using polyanionic polysaccharides, and belongs to the field of agricultural product processing and comprehensive utilization of by-products. Background technique [0002] Soy whey protein is the protein that remains in soybean whey and cannot be precipitated by acid. In soybean whey protein, the 2S component accounts for a large proportion; whey protein not only contains globulin and albumin, but also Mainly contains: ①Kunitz trypsin inhibitor (KTI, pH3.0~10.0, 20kDa); ②Bowman-Brik trypsin inhibitor (BBI, pH3.0~10.0, 20KDa); ③β-amylase (61.7KDa); ④Agglutination (pH2.2~10.8, 120KDa); ⑤Lipoxygenase (LOX, 102KDa) and other physiologically active substances account for 9%-15.3% of soybean protein. [0003] In medicine and biology, inhibitors have become useful tools in the study of pr...

Claims

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Application Information

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IPC IPC(8): C07K14/81C07K1/36C07K1/34C07K1/32C07K1/30
CPCC07K14/811C07K14/8114
Inventor 张彩猛华欲飞李兴飞孔祥珍陈业明
Owner JIANGNAN UNIV
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