TY - JOUR
T1 - Advances in enzyme stability modification
AU - Feng, Xudong
AU - Lü, Bo
AU - Li, Chun
N1 - Publisher Copyright:
© All Right Reserved.
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Enzymes play an increasingly important role in diverse industrial fields such as food, pharmacy and fine chemistry. However, most of the enzymes require mild reaction conditions to maintain the activity, and they have poor tolerance towards heat, acid and salt under stressful conditions in real applications. Thus, the enzymes are very labile to lose their activity, severely limiting their applications. Therefore, it is critical and also challenging to engineer enzymes for higher stability. In this paper, the progress in enzyme stability modification is summarized from perspectives of chemical decoration and molecular modification. The molecular modification is illustrated with regards to directed evolution, semi-rational, ration design and glycosylation, where the glycosylation as a new tool to improve enzyme stability is briefly reviewed.
AB - Enzymes play an increasingly important role in diverse industrial fields such as food, pharmacy and fine chemistry. However, most of the enzymes require mild reaction conditions to maintain the activity, and they have poor tolerance towards heat, acid and salt under stressful conditions in real applications. Thus, the enzymes are very labile to lose their activity, severely limiting their applications. Therefore, it is critical and also challenging to engineer enzymes for higher stability. In this paper, the progress in enzyme stability modification is summarized from perspectives of chemical decoration and molecular modification. The molecular modification is illustrated with regards to directed evolution, semi-rational, ration design and glycosylation, where the glycosylation as a new tool to improve enzyme stability is briefly reviewed.
KW - Biocatalysis
KW - Biochemical engineering
KW - Enzyme
KW - Glycosylation
KW - Molecular modification
KW - Stability
UR - http://www.scopus.com/inward/record.url?scp=85092427108&partnerID=8YFLogxK
U2 - 10.11949/j.issn.0438-1157.20151025
DO - 10.11949/j.issn.0438-1157.20151025
M3 - Article
AN - SCOPUS:85092427108
SN - 0438-1157
VL - 67
SP - 277
EP - 284
JO - Huagong Xuebao/CIESC Journal
JF - Huagong Xuebao/CIESC Journal
IS - 1
ER -