CN114149744A - High-strength salting-out-resistant efflorescence-resistant bio-based seal primer and construction method - Google Patents

High-strength salting-out-resistant efflorescence-resistant bio-based seal primer and construction method Download PDF

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CN114149744A
CN114149744A CN202111555967.2A CN202111555967A CN114149744A CN 114149744 A CN114149744 A CN 114149744A CN 202111555967 A CN202111555967 A CN 202111555967A CN 114149744 A CN114149744 A CN 114149744A
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buffer solution
amyloid
reducing agent
resistant
disulfide bond
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CN114149744B (en
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李游亚
潘建中
王燕
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Caparol China Co ltd
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    • CCHEMISTRY; METALLURGY
    • C09DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
    • C09DCOATING COMPOSITIONS, e.g. PAINTS, VARNISHES OR LACQUERS; FILLING PASTES; CHEMICAL PAINT OR INK REMOVERS; INKS; CORRECTING FLUIDS; WOODSTAINS; PASTES OR SOLIDS FOR COLOURING OR PRINTING; USE OF MATERIALS THEREFOR
    • C09D189/00Coating compositions based on proteins; Coating compositions based on derivatives thereof
    • CCHEMISTRY; METALLURGY
    • C09DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
    • C09DCOATING COMPOSITIONS, e.g. PAINTS, VARNISHES OR LACQUERS; FILLING PASTES; CHEMICAL PAINT OR INK REMOVERS; INKS; CORRECTING FLUIDS; WOODSTAINS; PASTES OR SOLIDS FOR COLOURING OR PRINTING; USE OF MATERIALS THEREFOR
    • C09D5/00Coating compositions, e.g. paints, varnishes or lacquers, characterised by their physical nature or the effects produced; Filling pastes
    • C09D5/002Priming paints
    • CCHEMISTRY; METALLURGY
    • C09DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
    • C09DCOATING COMPOSITIONS, e.g. PAINTS, VARNISHES OR LACQUERS; FILLING PASTES; CHEMICAL PAINT OR INK REMOVERS; INKS; CORRECTING FLUIDS; WOODSTAINS; PASTES OR SOLIDS FOR COLOURING OR PRINTING; USE OF MATERIALS THEREFOR
    • C09D7/00Features of coating compositions, not provided for in group C09D5/00; Processes for incorporating ingredients in coating compositions
    • C09D7/40Additives
    • C09D7/60Additives non-macromolecular
    • C09D7/63Additives non-macromolecular organic
    • EFIXED CONSTRUCTIONS
    • E04BUILDING
    • E04BGENERAL BUILDING CONSTRUCTIONS; WALLS, e.g. PARTITIONS; ROOFS; FLOORS; CEILINGS; INSULATION OR OTHER PROTECTION OF BUILDINGS
    • E04B1/00Constructions in general; Structures which are not restricted either to walls, e.g. partitions, or floors or ceilings or roofs
    • E04B1/62Insulation or other protection; Elements or use of specified material therefor
    • E04B1/66Sealings
    • EFIXED CONSTRUCTIONS
    • E04BUILDING
    • E04BGENERAL BUILDING CONSTRUCTIONS; WALLS, e.g. PARTITIONS; ROOFS; FLOORS; CEILINGS; INSULATION OR OTHER PROTECTION OF BUILDINGS
    • E04B1/00Constructions in general; Structures which are not restricted either to walls, e.g. partitions, or floors or ceilings or roofs
    • E04B1/62Insulation or other protection; Elements or use of specified material therefor
    • E04B1/92Protection against other undesired influences or dangers
    • EFIXED CONSTRUCTIONS
    • E04BUILDING
    • E04FFINISHING WORK ON BUILDINGS, e.g. STAIRS, FLOORS
    • E04F13/00Coverings or linings, e.g. for walls or ceilings
    • E04F13/02Coverings or linings, e.g. for walls or ceilings of plastic materials hardening after applying, e.g. plaster

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  • Engineering & Computer Science (AREA)
  • Chemical & Material Sciences (AREA)
  • Architecture (AREA)
  • Wood Science & Technology (AREA)
  • Civil Engineering (AREA)
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  • Life Sciences & Earth Sciences (AREA)
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  • Organic Chemistry (AREA)
  • Electromagnetism (AREA)
  • Physics & Mathematics (AREA)
  • Peptides Or Proteins (AREA)
  • Application Of Or Painting With Fluid Materials (AREA)

Abstract

The invention belongs to the field of building material exterior wall coatings, and discloses a high-strength salting-out-resistant and efflorescence-resistant bio-based seal primer and a construction method. The primer comprises the components of A component and B component; the component B comprises a disulfide bond reducing agent buffer solution and an amyloid protein buffer solution; the component A is a protein film crosslinking solvent. The micro-nano composite structure formed by the phase transition of the amyloid aggregation primer system has larger bonding area and stronger bonding effect with the outer wall middle coating and the outer wall base layer.

Description

High-strength salting-out-resistant efflorescence-resistant bio-based seal primer and construction method
Technical Field
The invention belongs to the field of building material exterior wall coatings, and particularly relates to a high-strength salting-out and efflorescence resistant bio-based seal primer and a construction method.
Background
Because the exterior wall coating is a semi-finished product, the exterior wall coating can show the best effect only by matching with primer, middle coating and finish coating and reasonable construction process. The priming paint is used for being opened from top to bottom, and is in direct contact with the traditional outer wall base layer such as concrete and cement mortar on one hand, and is used together with the outer wall middle coating and finish coating on the other hand. In the face of such a complex environment, the primer has higher strength firstly, so that firm adhesion is provided for the outer wall primer, the phenomena of peeling and falling of the coating are prevented, and meanwhile, the problem that a paint film of the separation seam is torn off by the masking paper is avoided; secondly, the primer needs to have alkali-resistant sealing property because the conventional exterior wall base layer mostly contains a large amount of alkali-alkali substances, and the primer, as a coating layer directly contacting with the base layer, must be chemically stable in an alkali environment. The sealing property means blocking capillary pores of the outer wall base layer, so that on one hand, the phenomena of whitening, mildewing and fading caused by evaporation and migration of saline-alkali substances in the outer wall base layer to the surface of the coating along with moisture are prevented, and on the other hand, moisture and air outside the wall body are prevented from entering the wall body to corrode the reinforcing steel bars; thirdly, the water absorption of the base layer of the outer wall needs to be reduced by the primer, so that the phenomenon of blooming caused by inconsistent drying rate of the outer wall paint is avoided; finally, the shorter the curing time required for the primer, the better to balance the contradiction between the construction period and the primer drying time.
At present, three major problems exist in the conventional alkali-resistant seal primer on the market. Firstly, the emulsion has poor alkali resistance and low emulsion content, so that the film forming efficiency of the emulsion is low, the emulsion is degraded in an alkaline environment, and the sealing effect of the primer is reduced; secondly, the water permeability resistance of the primer is poor, the water on the surface of the wall body permeates into the base layer to damage the structure, and the water on the base layer permeates into the surface of the wall body to cause whitening along with the migration of saline-alkali substances; and thirdly, the adhesion between the primer and the base layer and the middle coating of the outer wall is poor, the primer is easy to stick and tear off by the masking paper, a proper amount of fine sand is added into the primer in production to improve the adhesion between the primer and the middle coating of the outer wall, and the addition of the fine sand can reduce the adhesion of the masking paper and increase the construction difficulty of the separation seam.
Inspired by the fact that organisms such as mussels, barnacles and bacteria can be firmly adsorbed on the surfaces of various materials, more and more interface bionic modification methods are proposed. For example, the polydopamine system reported by the northwest university of the united states in 2007 and the tannin-iron (III) complex system reported by the melbourne university of australia in 2013 both utilize covalent crosslinking of ortho-phenolic derivatives and non-covalent bonds such as van der waals forces and hydrogen bonds to be firmly immobilized on the interface. However, they cannot be used in primers because of their poor alkali resistance and long curing time.
The aggregation of amyloid is firstly found in the diseased kidney of a human body, and then the amyloid can be mistaken for an amyloid structure due to iodine staining, and barnacles and bacteria are firmly adsorbed on various material interfaces by the principle of the aggregation of the amyloid.
Therefore, there is a need to provide a new high-strength anti-salting-out and anti-efflorescence seal primer product to solve the problems of the conventional anti-alkali seal primers on the market.
Disclosure of Invention
The invention aims to provide a high-strength salting-out-resistant efflorescence-resistant bio-based seal primer and a construction method aiming at the defects of the prior art. The micro-nano composite structure formed by the phase transition of the amyloid aggregation primer system has larger bonding area and stronger bonding effect with the outer wall middle coating and the outer wall base layer.
In order to achieve the above object, the present invention provides, in one aspect, a high-strength salting-out-resistant alkali-efflorescence-based sealer comprising a composition comprising an a-component and a B-component;
the component B comprises a disulfide bond reducing agent buffer solution and an amyloid protein buffer solution;
the component A is a protein film crosslinking solvent.
According to the present invention, it is preferable that,
the disulfide bond reducing agent buffer solution comprises a disulfide bond reducing agent and an electrostatic shielding buffer solution;
the amyloid buffer comprises amyloid and an electrostatic shielding buffer solution;
the electrostatic shielding buffer solution contains a buffer substance and an electrostatic shielding compound.
According to the present invention, preferably, the method for preparing the disulfide bond reducing agent buffer comprises: and (3) mixing the disulfide bond reducing agent with the electrostatic shielding buffer solution to obtain the disulfide bond reducing agent buffer solution, and storing the disulfide bond reducing agent buffer solution in a non-illumination environment at 4-5 ℃.
According to the present invention, preferably, the preparation method of the amyloid buffer comprises: and mixing the amyloid with an electrostatic shielding buffer solution to obtain the amyloid buffer solution.
According to the present invention, preferably, the method for preparing the electrostatic shielding buffer solution comprises: mixing a buffer substance with water to obtain a buffer solution, adjusting the pH of the buffer solution to 7-9, preferably 7.2-8.5, and more preferably 7.4-8, and mixing the buffer solution with an electrostatic shielding compound to obtain an electrostatic shielding buffer solution; preferably, the method of adjusting the pH of the buffer solution comprises: the pH of the buffer solution is adjusted using an aqueous NaOH solution having a molar concentration of 0.5-1M.
According to the present invention, preferably, the disulfide bond reducing agent is at least one of tris (2-carboxyethyl) phosphine, L-cysteine, dithiothreitol, thioglycolic acid, ethanedithiol, and mercaptosuccinic acid.
According to the present invention, preferably, the amyloid is at least one of lysozyme, bovine serum albumin, insulin and α -lactalbumin.
According to the present invention, preferably, the buffer substance is at least one of HEPES, TAPS, TES, MOPS, PIPES, and MES.
According to the present invention, preferably, the electrostatic shielding compound is a salt, preferably, the salt is sodium chloride and/or sodium sulfate.
According to the present invention, preferably, when the disulfide bond reducing agent is tris (2-carboxyethyl) phosphine, the molar concentration of the tris (2-carboxyethyl) phosphine in the disulfide bond reducing agent buffer is 0.01 to 0.2M;
according to the present invention, preferably, when the disulfide bond reducing agent is any one of L-cysteine, dithiothreitol, thioglycolic acid, ethanedithiol, and mercaptosuccinic acid, the molar concentrations of the L-cysteine, dithiothreitol, thioglycolic acid, ethanedithiol, and mercaptosuccinic acid in the disulfide bond reducing agent buffer solution are each independently 0.03 to 0.15M.
According to the present invention, preferably, the mass concentration of the amyloid in the amyloid buffer is 2-10 g/L;
according to the invention, the molar concentration of the buffer substance in the buffer solution is preferably 8-16mM, preferably 10-12 mM.
According to the present invention, preferably, the molar concentration of the electrostatic shielding compound in the buffer solution is 50 to 150 mM.
According to the present invention, preferably, the volume ratio of the disulfide bond reducing agent buffer to the amyloid buffer is (1-1.2): 1.
According to the present invention, preferably, the protein film crosslinking solvent is prepared by dissolving a phenolic substance in water and oxidizing.
According to the present invention, preferably, the preparation method of the protein film crosslinking solvent comprises: mixing the phenolic substances with water at the temperature of 40-60 ℃ to obtain a mixed solution, adjusting the pH of the mixed solution to 8.8-9.2, and introducing oxygen into the mixed solution to obtain the protein film crosslinking solvent.
According to the invention, preferably, the time for introducing oxygen into the mixed solution is 2-5 h;
according to the present invention, preferably, the phenolic substance is at least one of caffeic acid, ferulic acid and tannic acid;
according to the invention, preferably, the amount of the phenolic substance is 5-10% of the mass of the amyloid protein, and the mass concentration of the phenolic substance in the mixed solution is 0.05-0.55 g/L;
according to the present invention, preferably, the method of adjusting the pH of the mixed solution includes: and adjusting the pH of the mixed solution by using a NaOH aqueous solution with the molar concentration of 0.5-1M.
The invention also provides a construction method of the high-strength salting-out-resistant saltpetering-alkali-resistant bio-based seal primer, which comprises the following steps:
s1: uniformly mixing the disulfide bond reducing agent buffer solution and the amyloid protein buffer solution to obtain an amyloid aggregation primer system;
s2: spraying the amyloid aggregation primer system on the surface of a constructed outer wall base layer to form a phase-transition protein film on the surface of the outer wall base layer;
s3: spraying the protein film crosslinking solvent on the phase-transition protein film to form the high-strength salting-out-resistant alkali-efflorescence-resistant bio-based seal primer.
In the present invention, in step S3, the high-strength anti-salting-out alkaloid-based sealing primer can be formed by spraying the protein film cross-linking solvent on the phase-transition protein film for 25-35 min.
According to the present invention, preferably, in step S1, the time for uniformly mixing the disulfide bond reducing agent buffer and the amyloid buffer is 10 to 15 min.
According to the present invention, it is preferable that the interval between the step S2 and the step S3 is 1.5-2.5 h.
In the invention, amyloid can undergo phase transition under the stimulation of a disulfide bond reducing agent buffer, during which the alpha-helical structure in the protein molecule is continuously converted to beta-sheet, so that the protein is rapidly converted from an initial dissolved state to insoluble amyloid-like aggregates to be separated out, and in the separation process, the amyloid buffer can form a large number of nano-scale oligomer particles, wherein one part of the nano-scale oligomer particles can further grow into fibrils and then are converted into micro-particles, and the other part of the nano-scale oligomer particles can form a layer of compact nano-film at a solid-liquid interface. The volume increase of the micro-nano particles and the formation of the nano film at the solid-liquid interface are in a mutual competitive relationship and are mainly influenced by the pH value in the amyloid buffer solution. When the pH of the solution is less than the isoelectric point pI of amyloid protein, the protonation degree of basic amino acid (such as arginine) in the protein is increased along with the reduction of the pH, the strong electron effect enables the molecular chain of the protein to be stably dispersed without aggregation, and the tendency of forming a micro-nano composite structure film is weakened; when the pH value of the solution is close to the isoelectric point pI of the amyloid protein, the protonation and ionization degree of unfolded amyloid protein is reduced, and the aggregation effect is increased, so that the unfolded amyloid protein is rapidly aggregated into particles; the phase transition process is very fast, and the aggregation of amyloid protein to form the final phase transition protein film can be completed within two hours under the control of the preparation conditions. In addition, the addition of electrostatic shielding compounds can weaken the electrostatic interaction between protein molecular chains, for example, the addition of salt solution can reduce the electrostatic repulsion between protein molecular chains and accelerate the aggregation of protein molecules. Therefore, in the process of amyloid protein aggregation, due to the multi-dimensionality, strong hydrogen bonds and electrostatic interaction of protein particles and close physical entanglement, the phase-change protein film formed by the method has excellent bonding strength.
In the present invention, the crosslinking in the molecular chain or between the molecules of the protein can be improved by using the protein film crosslinking solvent, and the strength and the water vapor blocking property of the phase transition protein film can be further increased, for example, the oxidized form (quinone) of the phenolic substance can be subjected to a crosslinking reaction with the active groups such as the thiol group on the cysteine residue and the free amino group in the protein molecule, so that the crosslinking in the molecular chain or between the molecules of the protein can be improved, and the strength and the water vapor blocking property of the phase transition protein film can be further increased.
The technical scheme of the invention has the following beneficial effects:
(1) the raw materials used in the invention belong to biological materials, are environment-friendly and pollution-free, and can realize zero VOC emission.
(2) The amyloid aggregation primer system is generated by continuously folding an alpha-helical structure in amyloid to beta-and is crosslinked through phenolic substances, so that the structure is stable and compact; hydrophobic tryptophan residues exist in the phase transition protein film, and water vapor is difficult to pass through; the multi-dimensionality, strong hydrogen bond and electrostatic action of the amyloid protein phase transition particles and close physical entanglement enable the phase transition protein film to have excellent bonding strength and can resist stripping of the textured paper.
(3) The micro-nano composite structure formed by the phase transition of the amyloid aggregation primer system has larger bonding area and stronger bonding effect with the outer wall middle coating and the outer wall base layer.
(4) The amyloid aggregation primer system is simple in production process, convenient to construct and operate and beneficial to industrialization.
Additional features and advantages of the invention will be set forth in the detailed description which follows.
Detailed Description
Preferred embodiments of the present invention will be described in more detail below. While the following describes preferred embodiments of the present invention, it should be understood that the present invention may be embodied in various forms and should not be limited by the embodiments set forth herein. Rather, these embodiments are provided so that this disclosure will be thorough and complete, and will fully convey the scope of the invention to those skilled in the art.
Example 1
The embodiment provides a high-strength salting-out-resistant alkali-efflorescence-based sealing primer which comprises the following components of a component A and a component B;
the component B comprises a disulfide bond reducing agent buffer solution and an amyloid protein buffer solution.
The disulfide bond reducing agent buffer solution comprises a disulfide bond reducing agent tris (2-carboxyethyl) phosphine and an electrostatic shielding buffer solution; the preparation method of the disulfide bond reducing agent buffer solution comprises the following steps: 9.00g of tris (2-carboxyethyl) phosphine was mixed with 500mL of an electrostatic shielding buffer solution to obtain the disulfide bond reducing agent buffer and stored in a non-light environment at 5 ℃.
The amyloid buffer solution comprises amyloid lysozyme and an electrostatic shielding buffer solution; the preparation method of the amyloid buffer solution comprises the following steps: 5g of lysozyme was mixed with 500mL of an electrostatic shielding buffer solution to obtain the amyloid buffer solution.
The electrostatic shielding buffer solution contains a buffer substance HEPES and an electrostatic shielding compound NaCl. The preparation method of the electrostatic shielding buffer solution comprises the following steps: 2.38g of HEPES (10mM) was mixed with 1000mL of distilled water to give a buffer solution and the pH of the buffer solution was adjusted to 7.5 by a 1M aqueous NaOH solution, and the buffer solution was further mixed with 2.92g of NaCl to give the electrostatic shielding buffer solution.
The volume ratio of the disulfide bond reducing agent buffer solution to the amyloid protein buffer solution is 1.2: 1.
The component A is a protein film crosslinking solvent. The preparation method of the protein film crosslinking solvent comprises the following steps: mixing 0.30g of ferulic acid with deionized water at 50 ℃ to obtain a mixed solution, adjusting the pH of the mixed solution to 9 by using a 1M NaOH aqueous solution, and introducing oxygen into the mixed solution for 3 hours to obtain the protein membrane crosslinking solvent.
The construction method of the high-strength salting-out-resistant alkali-efflorescence-resistant bio-based seal primer comprises the following steps:
s1: uniformly mixing the disulfide bond reducing agent buffer solution and the amyloid protein buffer solution for 10min to obtain an amyloid aggregation primer system;
s2: spraying the amyloid aggregation primer system on the surface of a constructed outer wall base layer, maintaining for 2 hours, and forming a phase-transition protein film on the surface of the outer wall base layer;
s3: and spraying the protein film crosslinking solvent on the phase-transition protein film, and forming the high-strength salting-out-resistant alkali-efflorescence-resistant bio-based sealing primer after 0.5 h.
Example 2
This example provides a high strength, salting-out resistant, efflorescent, alkaloid based primer sealer which differs from example 1 only in that:
the disulfide bond reducing agent buffer solution is prepared by mixing 7.20g of tris (2-carboxyethyl) phosphine with 500mL of electrostatic shielding buffer solution, and the disulfide bond reducing agent buffer solution is stored in a non-illumination environment at 5 ℃.
The amyloid buffer solution is obtained by mixing 2g of lysozyme with 500mL of electrostatic shielding buffer solution.
The electrostatic shielding buffer solution is prepared by mixing 2.38g HEPES (10mM) with 1000mL distilled water to obtain a buffer solution, adjusting the pH of the buffer solution to 7.5 by 1M NaOH aqueous solution, and mixing the buffer solution with 3.55g Na2SO4And mixing to obtain the electrostatic shielding buffer solution.
The volume ratio of the disulfide bond reducing agent buffer solution to the amyloid protein buffer solution is 1: 1.
The protein film crosslinking solvent is obtained by mixing 0.10g of caffeic acid with deionized water at 50 ℃ to obtain a mixed solution, adjusting the pH of the mixed solution to 9 by using 0.5M NaOH aqueous solution, and introducing oxygen into the mixed solution for 3 hours.
Example 3
This example provides a high strength, salting-out resistant, efflorescent, alkaloid based primer sealer which differs from example 1 only in that:
the disulfide bond reducing agent buffer solution is prepared by mixing 6.06g L-cysteine with 500mL of electrostatic shielding buffer solution, and storing at 5 ℃ in a non-illumination environment.
The amyloid buffer solution is obtained by mixing 5g of insulin with 500mL of electrostatic shielding buffer solution.
The electrostatic shielding buffer solution is prepared by mixing 2.38g of HEPES (10mM) with 1000mL of distilled water to obtain a buffer solution, adjusting the pH of the buffer solution to 7.5 by using a 1M NaOH aqueous solution, and mixing the buffer solution with 5.00g of NaCl.
The volume ratio of the disulfide bond reducing agent buffer solution to the amyloid protein buffer solution is 1: 1.
The protein film crosslinking solvent is obtained by mixing 0.50g of caffeic acid with deionized water at 50 ℃ to obtain a mixed solution, adjusting the pH of the mixed solution to 9 by using 0.5M NaOH aqueous solution, and introducing oxygen into the mixed solution for 3 hours.
Test example
This test example the high strength salting-out resistant alkali-efflorescence-based sealer primers formed in examples 1 to 3 were subjected to respective performance tests, and the test results are shown in Table 1.
TABLE 1
Figure BDA0003418693900000091
Having described embodiments of the present invention, the foregoing description is intended to be exemplary, not exhaustive, and not limited to the embodiments disclosed. Many modifications and variations will be apparent to those of ordinary skill in the art without departing from the scope and spirit of the described embodiments.

Claims (10)

1. The high-strength salting-out-resistant alkali-efflorescence-resistant bio-based seal primer is characterized in that the primer comprises a component A and a component B;
the component B comprises a disulfide bond reducing agent buffer solution and an amyloid protein buffer solution;
the component A is a protein film crosslinking solvent.
2. The high strength salting-out resistant saltpetering-out alkaloid based washcoat of claim 1, wherein,
the disulfide bond reducing agent buffer solution comprises a disulfide bond reducing agent and an electrostatic shielding buffer solution;
the amyloid buffer comprises amyloid and an electrostatic shielding buffer solution;
the electrostatic shielding buffer solution contains a buffer substance and an electrostatic shielding compound.
3. The high strength, salting-out resistant, saltpetering alkaloid based washcoat of claim 2,
the preparation method of the disulfide bond reducing agent buffer solution comprises the following steps: mixing a disulfide bond reducing agent with an electrostatic shielding buffer solution to obtain a disulfide bond reducing agent buffer solution, and storing the disulfide bond reducing agent buffer solution in a non-illumination environment at 4-5 ℃;
the preparation method of the amyloid buffer solution comprises the following steps: mixing amyloid with an electrostatic shielding buffer solution to obtain an amyloid buffer solution;
the preparation method of the electrostatic shielding buffer solution comprises the following steps: mixing a buffer substance with water to obtain a buffer solution, adjusting the pH value of the buffer solution to 7-9, and mixing the buffer solution with an electrostatic shielding compound to obtain the electrostatic shielding buffer solution;
preferably, the method of adjusting the pH of the buffer solution comprises: the pH of the buffer solution is adjusted using an aqueous NaOH solution having a molar concentration of 0.5-1M.
4. The high strength, salting-out resistant, saltpetering alkaloid based washcoat of claim 2,
the disulfide bond reducing agent is at least one of tri (2-carboxyethyl) phosphine, L-cysteine, dithiothreitol, thioglycolic acid, ethanedithiol and mercaptosuccinic acid;
the amyloid is at least one of lysozyme, bovine serum albumin, insulin and alpha-lactalbumin;
the buffer substance is at least one of HEPES, TAPS, TES, MOPS, PIPES and MES;
the electrostatic shielding compound is a salt, preferably the salt is sodium chloride and/or sodium sulfate.
5. The high strength salting-out resistant saltpetering-out alkaloid based washcoat of claim 4, wherein,
when the disulfide bond reducing agent is tris (2-carboxyethyl) phosphine, the molar concentration of the tris (2-carboxyethyl) phosphine in the disulfide bond reducing agent buffer is 0.01-0.2M;
when the disulfide bond reducing agent is any one of L-cysteine, dithiothreitol, thioglycolic acid, ethanedithiol and mercaptosuccinic acid, the molar concentrations of the L-cysteine, the dithiothreitol, the thioglycolic acid, the ethanedithiol and the mercaptosuccinic acid in the disulfide bond reducing agent buffer solution are respectively and independently 0.03-0.15M;
the mass concentration of the amyloid in the amyloid buffer solution is 2-10 g/L;
the molar concentration of the buffer substance in the buffer solution is 8-16mM, preferably 10-12 mM;
the molar concentration of the electrostatic shielding compound in the buffer solution is 50-150 mM.
6. The high-strength anti-salting-out ubiquinone-based sealer according to any one of claims 1 to 5, wherein a volume ratio of the disulfide reducing agent buffer to the amyloid buffer is (1-1.2): 1.
7. The high strength, salting-out resistant, saltpetering alkaloid based washcoat of claim 2, wherein the protein film crosslinking solvent is prepared from phenolic species dissolved in water and oxidized.
8. The high strength, salting-out resistant, saltpetering alkaloid based primer sealer according to claim 7, wherein the protein film crosslinking solvent is prepared by a method comprising: mixing phenolic substances with water at 40-60 ℃ to obtain a mixed solution, adjusting the pH of the mixed solution to 8.8-9.2, and introducing oxygen into the mixed solution to obtain the protein film crosslinking solvent;
preferably, the time for introducing oxygen into the mixed solution is 2-5 h;
preferably, the phenolic substance is at least one of caffeic acid, ferulic acid and tannic acid;
preferably, the dosage of the phenolic substance is 5-10% of the mass of the amyloid protein, and the mass concentration of the phenolic substance in the mixed solution is 0.05-0.55 g/L;
preferably, the method of adjusting the pH of the mixed solution includes: and adjusting the pH of the mixed solution by using a NaOH aqueous solution with the molar concentration of 0.5-1M.
9. The method of applying the high-strength salting-out-resistant saltpetering-out-overthe-alkali-based sealer as claimed in any one of claims 1 to 8, comprising:
s1: uniformly mixing the disulfide bond reducing agent buffer solution and the amyloid protein buffer solution to obtain an amyloid aggregation primer system;
s2: spraying the amyloid aggregation primer system on the surface of a constructed outer wall base layer to form a phase-transition protein film on the surface of the outer wall base layer;
s3: spraying the protein film crosslinking solvent on the phase-transition protein film to form the high-strength salting-out-resistant alkali-efflorescence-resistant bio-based seal primer.
10. The method of applying a high-strength salting-out-resistant saltpetering-out-inhibiting alkaloid based sealer according to claim 9,
in step S1, the time for uniformly mixing the disulfide bond reducing agent buffer and the amyloid buffer is 10-15 min;
the time interval between the step S2 and the step S3 is 1.5-2.5 h.
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