Preparation method of edible collagen membrane

Abstract

The invention discloses a preparation method of an edible collagen membrane. The method comprises the following steps: first, performing a reaction on animal collagen dissolved by an acetic acid solution and hydroxycarboxylic acid-N-hydroxysuccinimide ester, removing bubbles, performing film forming and drying to obtain a transparent collagen membrane, soaking the obtained transparent collagen membrane in a solution containing oxidase for a reaction, after the reaction is finished, performing washing by water and performing drying to obtain the edible collagen membrane. In the method provided by the invention, with the adoption of step-by-step crosslinking modification on a collagen membrane, the system is uniform in crosslinking, the membrane is more uniform and compact, and the crosslinking degree is higher, so that the tensile strength of the membrane can be greatly improved, and meanwhile, the membrane is transparent in color, and is more suitable for being used as a packaging material for highlighting the color of packaged objects. The method provided by the invention is simple in method and easy in operation and is easy for popularization and application.

Description

technical field [0001] The invention belongs to the technical field of preparation of collagen films, and in particular relates to a preparation method of edible collagen films. Background technique [0002] In recent years, people have been devoting themselves to the development of new degradable and low-cost food packaging materials. Due to the incomparable superiority of other materials, collagen membrane has gradually attracted people's attention. Collagen film is made according to the excellent film-forming properties of collagen. Because collagen not only has a tight triple helical structure, it can endow the collagen film with a certain toughness and strength after film formation, but also collagen itself has immobilized enzymes. The function can improve the flavor and quality of food to a certain extent. In addition, the collagen film is rich in amino acids needed by the human body. People can also supplement various rich amino acids while eating and the raw materia...

AI Technical Summary

Problems solved by technology

Although the combination of glutaraldehyde modification and thermal crosslinking greatly increases the denaturation temperature of collagen casings, glutaraldehyde, as an exogenous substance, has certain cytotoxicity, and the modified collagen film will appear light yellow , which in turn affects the appearance of the packaging film

Xie Shuzhong et al. (Xie Shuzhong, Li Guoying. Preparation of a kind of malonic acid derivative and its application to the modification of collagen film[J]. China Leather, 2011,40(15):32~34.) Soaked cowhide collagen film Soak in a solution of NHS malonate with a pH of 7.0 in different concentrations (5g / L, 10g / L, 15g / L) for 1h, rinse the surface with water after the reaction, and the test results after drying show that when the concentration is At 15g / L, the tensile strength of the collagen film increases the most, which can reach 1.98 times that of the unmodified collagen film. However, due to the method of soaking and cross-linking, most of the cross-linking agents are combined on the surface of the collagen film, making it difficult to enter The interior of the collagen membrane, resulting in a low degree of cross-linking and limited contribution to the tensile strength of the collagen membrane; Tetsushi Taguchi et al. (Tetsushi Taguchi, Hirofuimi Saito, Yoshiyuki Uchida, et al. consisting of a citric acid derivative and collagen[J].MaterialsScience and Engieering,2004,24:775~780.) Using citric acid derivatives (ie citric acid-N-hydroxysuccinimide ester) to react with porcine cartilage tissue, As the concentration of the crosslinking agent increases, the bonding strength also increases, and finally it can only reach 80% of the strength after modification of the traditional crosslinking agent, and the cytotoxicity of the modifier is only ten times that of glutaraldehyde and formaldehyde. 1 / 1, and can be degraded in 7 days in living animals

Although citric acid derivatives, as a cross-linking agent with low toxicity, can be degraded in the human body and can be used as implant materials in the medical field, the improvement of the mechanical properties of materials is not as great as that of conventional cross-linking agents.

Jeevithan Elango et al. Make 1% catfish skin collagen with 0.3M acetic acid, then add 0.55% glutamine transaminase and 0.55% glutaraldehyde respectively to the two identical collagen solutions, stir the reaction, and then put them under the condition of 30 ℃ After forming a film, the enzyme-modified film and the glutaraldehyde-modified film were obtained by drying. The results showed that the glutaraldehyde-modified film was light yellow, and the tensile strength increased from 2.3MPa to 3.8MPa, while the transglutaminase modified The permanent film is white and transparent, and the tensile strength increases from 2.3MPa to 6.4MPa, which means that food-grade transglutaminase cross-linked catfish skin collagen can increase the tensile strength of the collagen film by 2.78 times, which is higher than that of glutaraldehyde-modified The improvement of the membrane is higher, but the improvement of the performance of the collagen membrane by a single enzyme modification is still limited, and it cannot fully meet the requirements for the tensile strength of the collagen membrane.

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