TY  - JOUR
AU  - Godoy, César A
AU  - Klett, Javier
AU  - Di Geronimo, Bruno
AU  - Hermoso, Juan A
AU  - Guisán, José M
AU  - Carrasco-López, César
PY  - 2019
DO  - 10.3390/ijms20215245
SN  - 1422-0067
UR  - http://hdl.handle.net/20.500.12105/9350
AB  - Enhancement, control, and tuning of hydrolytic activity and specificity of lipases are major goals for the industry. Thermoalkaliphilic lipases from the I.5 family, with their native advantages such as high thermostability and tolerance to alkaline...
LA  - eng
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
KW  - Engineered disulfide bond
KW  - Engineered lipase
KW  - Interfacial activation
KW  - Lipases activity enhancement
KW  - Thermoalkaliphilic lipase
KW  - Amino Acid Substitution
KW  - Bacterial Proteins
KW  - Cysteine
KW  - Disulfides
KW  - Enzyme Stability
KW  - Enzymes, Immobilized
KW  - Geobacillus
KW  - Lipase
KW  - Molecular Dynamics Simulation
KW  - Catalytic Domain
TI  - Disulfide Engineered Lipase to Enhance the Catalytic Activity: A Structure-Based Approach on BTL2
TY  - journal article
ER  -