𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Improvement of the activity of arylmalonate decarboxylase by random mutagenesis

✍ Scribed by Y. Terao; K. Miyamoto; H. Ohta


Publisher
Springer
Year
2006
Tongue
English
Weight
159 KB
Volume
73
Category
Article
ISSN
1432-0614

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Improving the functional expression of a
✍ Katja Koschorreck; Rolf D Schmid; Vlada B Urlacher πŸ“‚ Article πŸ“… 2009 πŸ› BioMed Central 🌐 English βš– 967 KB

## Abstract ## Background Laccases have huge potential for biotechnological applications due to their broad substrate spectrum and wide range of reactions they are able to catalyze. These include, for example, the formation and degradation of dimers, oligomers, polymers, and ring cleavage as well

Improvement of low-temperature caseinoly
✍ Chuan-Qi Zhong; Shengli Song; Nan Fang; Xiaoliang Liang; Hui Zhu; Xiao-Feng Tang πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 442 KB πŸ‘ 1 views

## Abstract By directed evolution and subsequent site‐directed mutagenesis, cold‐adapted variants of WF146 protease, a thermophilic subtilase, have been successfully engineered. A four‐amino acid substitution variant RTN29 displayed a sixfold increase in caseinolytic activity in the temperature ran