Computational analysis of di-peptides correlated with the optimal temperature in G/11 xylanase

The di-peptides positively correlated with optimal temperature in G/11 xylanase are computed to be: LA, LG, CD, GD, RY, CH; the negatively ones are: DC, YI, YP, and CP. The comparison of the structures of mesophilic and thermophilic xylanase showed that these di-peptides predominantly occur in beta-turns. These results explain the successful improvement of thermostability by introducing arginines into the xylanase surface area and therefore have implications for xylanase engineering.