Related Experiment Video
Updated: Dec 18, 2025

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Remarks on Computational Method for Identifying Acid and Alkaline Enzymes
Hongfei Li1, Haoze Du2, Xianfang Wang1
1School of Computer and Information Engineering, Henan Normal University, Xinxiang 453007, China.
Abstract:
The catalytic efficiency of the enzyme is thousands of times higher than that of ordinary catalysts. Thus, they are widely used in industrial and medical fields. However, enzymes with protein structure can be destroyed and inactivated in high temperature, over acid or over alkali environment. It is well known that most of enzymes work well in an environment with pH of 6-8, while some special enzymes remain active only in an alkaline environment with pH > 8 or an acidic environment with pH < 6. Therefore, the identification of acidic and alkaline enzymes has become a key task for industrial production. Because of the wide varieties of enzymes, it is hard work to determine the acidity and alkalinity of the enzyme by experimental methods, and even this task cannot be achieved. Converting protein sequences into digital features and building computational models can efficiently and accurately identify the acidity and alkalinity of enzymes. This review summarized the progress of the digital features to express proteins and computational methods to identify acidic and alkaline enzymes. We hope that this paper will provide more convenience, ideas, and guides for computationally classifying acid and alkaline enzymes.
Related Concept Videos
Diagnosing Acidosis and Alkalosis
First, the pH level is assessed to determine whether the blood pH is normal (7.35–7.45), low (acidosis), or high (alkalosis).
Next, the PCO2 and...
Titration of Polyprotic Base with a Strong Acid
Titration of a Weak Acid with a Strong Base
Solution Composition During Acid/Base Titrations
The α0 and α1 values...
Titration of a Weak Acid with a Weak Base
As a result, there is no simple...

