Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31401637]
机构署名：
本校为第一且通讯机构
院系归属：
生物科学技术学院
摘要：
BACKGROUNDThe disordered residues on distal loops affect the molecular structural stability and on some occasions have regulatory roles in catalytic reaction. To increase understanding of the influence of distal residue mutation, this study explored the thermostability and enzymatic activity of mannanase Man1312 deletion mutants. The focus was on residues located on the N-terminal region because they are more disordered and changeable. The effects of N-terminal truncation on enzymatic activity and thermal dynamics were investigated by spectrophotometry, circular dichroism and differential scan...
