Difference between revisions of "Team:AHUT China/design"

As we have described in the background, traditional carbon dioxide collection techniques are still in its early stages, characterized by high consumption and low efficiency. We want low-energy, large-scale, efficient collection of carbon dioxide, in order to achieve this goal, we by the carbon anhydride enzyme gene into E. coli.

To ensure that E. coli-producing carbonic anhydride (CA-II) normally absorbs carbon dioxide in an industrialized environment, we first simulate the protein molecule expressed by a computer to obtain a thermally stable carbonic anhydride (CA-II), which produces a thermally stable carbonic anhydride (CA-II), so that it can normally absorb carbon dioxide in a factory-like environment.

E. Coli's carbonic anhydride enzyme (CA-II) promotes CO2 hydration to produce co32-, which binds to the free ca2+ in the environment to form calcium carbonate deposits, thereby achieving the purpose of absorbing carbon dioxide, and producing inorganic products that can be used.

Selection of carbonic anhydride enzymes:
Our team acquired a sequence of the human Body's carbonic anhydride, and contacted biotech companies to help us synthesize the carbonic anhydride gene in full sequence. The Carbon-anhydride (CA-II) activity of the human being used by our team is more active than that of other mammals, plants, algae, and bacteria-producing carbonic anhydride (CA-II). The carbon anhydride (CA-II) extracted in the human body at 37 ℃ the fastest reaction rate, 50 ℃ conditions, But its maximum reaction rate can reach 106 s-1, the fastest catalytic rate of carbonic anhydride (CA-II).

Carbonic anhydride Enzyme structure:

ＣＨＲＩＳＴＯＰＨＥＲＫＳ，ＪＡＭＥＳＪＬ．Ｂｉｏｔｅｃｈｎｏｌｏｇｙｆｏｒ ｔｈｅａｃｃｅｌｅｒａｔｉｏｎｏｆｃａｒｂｏｎｄｉｏｘｉｄｅｃａｐｔｕｒｅａｎｄｓｅｑｕｅｓ－ ｔｒａｔｉｏｎ［Ｊ］．ＳｃｉｅｎｃｅＤｉｒｅｃｔ，２０１１，２２：８１８－８２３．

Increased thermal stability of carbonic anhydride (CA-II):

In order to make the carbonic anhydride enzyme (CA-II) suitable for the industrial environment to absorb carbon dioxide, later we use molecular simulation technology, the amino acid as the basic unit, the residual radical mutation on the two-stage structure of carbon anhydride, and the influence of molecular conformation, to obtain the best amino acid mutation sites, The thermal stability of enzymes was improved without affecting the enzyme Activity.
Note: This part also the experimental data of the thermal stability of the carbon anhydride enzyme and the three-dimensional map of the fixed-point mutant base of the carbonic anhydride gene have not been added and referenced

The mechanism of hydration of carbon dioxide catalyzed by carbonic anhydride enzyme (CA-II:

Duda D, Tu C , Qian M, et al , 2001.Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic an- hydrase Ⅱ [ J] .Biochemistry , 40 (6):1741—1748

Elder I , Han S , Tu C , et al , 2004.Activation of carbonic anhydrase Ⅱ by active-site incorporation of histidine analogs [ J] .Arc Bioch Biophys, 421:283—289

Application of carbonic anhydride enzyme (ca-ii) in carbon dioxide concentration

There are two kinds of enzymatic trapping techniques: non-immobilized carbon anhydride trapping technology and immobilized carbon anhydride trapping technology. Non-immobilized Carbon anhydride trapping technology is the first carbon anhydride capture technology, This method directly using free carbon anhydride enzyme CO2 capture, at this time the activity of carbonic anhydride enzyme is low, about 30% of the activity, and this method is not conducive to the re-use of enzymes; in order to compensate for the deficiency of non-immobilized carbonic anhydride enzyme technology, Some people will silica and other inorganic compounds as a carrier of the carbon anhydride enzyme, thereby curing the carbon anhydride enzyme, it is found that the activity of carbon anhydride at this time to maintain about 60%, and the easy recovery of carbonic anhydride enzyme, so our team is using immobilized carbon anhydride enzyme capture technology.

Reference documentation

S L. Structure and mechanism of carbonic anhydrase [J]. Pharmacology & Therapeutics, 1997, 74(1): 1. Supuran C T, Conroy C W, Maren T H. Is cyanate a carbonic anhydrase substrate? [J]. Proteins-structure Function & Bioinformatics, 2015, 27(2): 272-8.