The crystal water affect in the interaction between the tenebrio molitor alpha-amylase and its inhibitor.

Molecular dynamics simulation of the interaction between the Tenebrio molitor alpha-amylase and its inhibitor at different proportion of crystal water was carried out with OPLS force field by hyperchem 7.5 software. In the correlative study, the optimal temperature of wheat monomeric and dimeric protein inhibitors was from 273 K to 318 K.

Related dipeptide and characteristic dipeptide of optimal pH in alpha-amylase.

Alpha-amylase is an enzyme of great significance to industry, but most alpha-amylases are unstable at lower pH. In this paper, we have studied the related dipeptide and characteristic dipeptide of optimal pH in alpha-amylase. On analysis, it gives the explicit results as follows: (1) Ten dipeptides are associated with alpha-amylase's optimal pH.