Method for extracting pectin by utilizing potato scraps
A potato and potato residue technology, applied in the field of potato pectin extraction, can solve the problems of not meeting the requirements of pectin quality and purity, high impurity macromolecular carbohydrate content, large aluminum residue, etc. The effect of lowering blood sugar and blood lipids and a large amount of raw materials
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specific Embodiment approach 1
[0010] Specific embodiment one: utilize the method for extracting pectin from potato residues in the present embodiment to carry out according to the following steps:
[0011] 1. Mix fresh potato residue and ultrapure water, wherein the mass ratio of fresh potato residue and pure water is 1:3, then add it into a homogenizer, and perform homogenization treatment at a speed of 10000r / min for 5 minutes to obtain potato residue The particle size of the potato residue in the potato residue slurry is 2-50 μm;
[0012] 2. Stir the potato slurry at a speed of 100~150r / min, adjust the pH value to 8~8.5, then add protease, react at 50~55°C for 3h, and heat at 0.4~0.6MPa steam pressure for 15~30min (full paste liquefaction), then add high temperature resistant α-amylase, adjust the pH value to 5.5~7, act at 90~95°C for 0.5h (to fully liquefy the starch), cool to 60°C, and then add α-1,4- Glucose hydrolase, adjust the pH value to 4~4.5, saccharify and hydrolyze at 60°C for 2 hours (so th...
specific Embodiment approach 2
[0015] Specific embodiment two: the difference between this embodiment and specific embodiment one is: the acid-base used for adjusting pH in step 2 is an inorganic acid-base, and the alkali is sodium hydroxide or sodium carbonate, and the acid is sulfuric acid or hydrochloric acid, and the concentration of the alkali is is 1 mol / L, and the acid concentration is 1 mol / L. Other steps and parameters are the same as those in the first embodiment.
specific Embodiment approach 3
[0016] Specific embodiment 3: This embodiment differs from specific embodiment 1 or 2 in that: the enzymatic activity of the protease described in step 2 is 200,000 U / g. Other steps and parameters are the same as those in Embodiment 1 or Embodiment 2.
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