TG Enzyme-Soy Protein Isolate
Cat.No:T9480 Solarbio
Storage:Store at RT,avoid moisture,1 year
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Storage:Store at RT,avoid moisture,1 year
Qty:
Size:
| Storage | Store at RT,avoid moisture,1 year |
| Enzyme Activity/Titer | 100U/g |
| Unit | Bottle |
| Specification | 500g |
Overview:
Transglutaminase, also known as transglutaminase (TG), is a transferase that catalyzes the acyl transfer reaction, which can catalyze the cross-linking between protein molecules and bond protein molecules. It acts on a variety of substrate proteins, such as soy protein, casein, gluten, actin, myosin, and so on, can significantly improve the gelability, solubility, emulsification and emulsification stability of soy protein, and then improve the nutritional value of protein, improve the flavor and taste of food, and prolong the storage period. Therefore, transglutaminase has a very wide range of applications in soybean product processing.
Product features:
1. Strong adhesive force. This product catalyzes the formation of a kind of ε- (Υ- glutamyl) lysyl covalent bond between protein molecules, which is difficult to break under normal non-enzymatic catalytic conditions. It can make protein molecules more closely together, improve the strength of soy protein gel, and make the soybean protein with high viscosity and good elasticity. It can improve the yield of soybean protein isolate.
2. Good pH stability. The optimum pH of TG was 6.0, but the enzyme had high activity in the pH range of 5.0-8.0.
3. Strong thermal stability. The optimal temperature of TG was 50 ℃, and the activity of TG was high in the range of 45 ℃ to 55 ℃. Especially in protein food systems, the thermostability of the enzyme can be significantly improved, which prevents its rapid inactivation during general food processing.
4. In the process of protein reaction catalyzed by TG, there was a negative correlation between temperature (within the temperature of maintaining enzyme activity) and time: higher reaction temperature, shorter reaction time; Conversely, the lower the temperature, the longer the time. The physical and chemical properties of different types of food determine the relationship between temperature and time during the reaction.
5. Green, safe and healthy. TG is widely found in animals, plants and microorganisms. People have been eating foods containing e-(G-glutamyl) lysine isopeptide bonds catalyzed by TG. Therefore, new foods produced and processed using TG are not only safe for human body, but also beneficial to human health.
Note:Product information may be optimized and upgraded. Please refer to the actual label information for accuracy.
Remark:These protocols are for reference only. Solarbio does not independently validate these methods.
Note:
1. The products are all for scientific research use only. Do not use it for medical, clinical diagnosis or treatment, food and cosmetics, etc. Do not store them in ordinary residential areas.
2. For your safety and health, please wear laboratory clothes, disposable gloves and masks.
3. The experimental results may be affected by many factors, after-sale service is limited to the product itself and does not involve other compensation.
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Improving gel properties of soy protein isolate through alkaline pH-shifting,mild heat treatment,and TGase cross-linking
Click to check >>Author:Ping Sun, Qin Zhang, Yu Zhao, Dongshun Zhao, Xiaohui Zhao, Lianzhou Jiang, Yan Zhang, Fei Wu, Xiaonan Sui
IF:11.5040
Publish_to:FOOD HYDROCOLLOIDS
PMID:
pH-Shifting combined with ultrasound treatment of emulsion-filled β-conglycinin gels as β-carotene carriers: Effect of emulsion concentration on gel properties
Click to check >>Author:Ziteng Lian, Sai Yang, Xinhui Peng, Xiaohong Tong, Mengmeng Wang, Shicheng Dai, Tingting Zhu, Huan Wang, Lianzhou Jiang
IF:9.3360
Publish_to:ULTRASONICS SONOCHEMISTRY
PMID:37086535
Effects of transglutaminase and glucose oxidase on the properties of frozen dough: Water distribution,rheological properties,and microstructure
Click to check >>Author:Wen-Tao Guo, Xue-Fei Yang, Yi-Shun Ji, Bin Hu, Wan-Guang Li, Xi-Yang Zhong, Shao-Tong Jiang, Zhi Zheng
IF:4.0750
Publish_to:JOURNAL OF CEREAL SCIENCE
PMID: