How to effectively ensure the activity of glutamate dehydrogenase 9029-12-3?

Glutamate dehydrogenase, as a key enzyme, plays an irreplaceable role in many fields such as biochemistry research and diagnosis. However, its activity is highly susceptible to external environmental factors, and how to properly preserve it to maintain its activity has become a challenge that practitioners in related fields must overcome. This article will delve into the preservation methods of glutamate dehydrogenase, providing practical guidelines to ensure its activity is not affected.

1. Low temperature environment

Under low temperature conditions, the thermal motion of enzyme molecules slows down and the chemical reaction rate decreases, effectively reducing enzyme denaturation and inactivation. Usually, storing glutamate dehydrogenase in a refrigerator at 4 ℃ for a short period of time (several days to several weeks) can maintain its relatively stable activity. If long-term storage (several months or even years) is required, an ultra-low temperature refrigerator at -20 ℃ or -80 ℃ should be selected. During low-temperature storage, it is important to avoid repeated freezing and thawing, as each freezing and thawing process can cause mechanical damage to enzyme molecules, leading to a decrease in activity. Suggest dividing the enzyme solution into small portions and taking out one portion each time to reduce the number of freeze-thaw cycles.

glutamate dehydrogenase

2. Buffer system

Choosing the appropriate buffer system is crucial for the preservation of glutamate dehydrogenase. Buffer solution can maintain the stability of the pH value of the solution, and even small changes in pH value may have a significant impact on enzyme activity. Generally speaking, glutamate dehydrogenase has higher and more stable activity in neutral or weakly alkaline environments with pH 7.0-8.0. Common buffer solutions include phosphate buffered saline (PBS), Tris HCl buffer, etc. When preparing buffer solutions, it is important to ensure that their ionic strength is appropriate. Excessive or insufficient ionic strength may affect the binding of enzymes to substrates.

3. Avoid oxidation and interference from metal ions

Oxidation and interference from metal ions are the two major "invisible killers" that cause the inactivation of glutamate dehydrogenase. Oxidants attack amino acid residues in enzyme molecules, disrupting their structure and function. Therefore, prolonged contact with air should be avoided during storage, and inert gases (such as nitrogen) can be used to replace the air inside the container. At the same time, certain metal ions such as copper ions, iron ions, etc. can catalyze oxidation reactions and accelerate enzyme inactivation. An appropriate amount of metal chelating agent, such as ethylenediaminetetraacetic acid (EDTA), can be added to the buffer solution to chelate metal ions in the solution and reduce their impact on enzyme activity.

4. Strict aseptic operation

Microbial contamination is also an important factor affecting the activity of glutamate dehydrogenase. Microorganisms produce various metabolites during their growth process, such as acids, bases, enzymes, etc. These substances can alter the pH and ionic strength of the solution, thereby affecting the activity of enzymes. Therefore, in the process of preserving glutamate dehydrogenase, strict adherence to aseptic operating procedures is necessary. Use sterile containers, reagents, and tools to operate in an ultra clean workbench, ensuring that the enzyme solution is not contaminated by microorganisms.

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