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1866551 
Journal Article 
Use of Protease from Bacillus licheniformis as Promiscuous Catalyst for Organic Synthesis: Applications in C-C and C-N Bond Formation Reactions 
Lopez-Iglesias, M; Busto, E; Gotor, V; Gotor-Fernandez, V 
2011 
1 
Advanced Synthesis & Catalysis
ISSN: 1615-4150
EISSN: 1615-4169 
353 
13 
2345-2353 
WOS:000295230900012 
Commercially available protease from Bacillus licheniformis has been used in different non-conventional biotransformations showing remarkable activity values. The promiscuous behaviour of this enzyme used in the cross-linked enzyme aggregates immobilized form (Alcalase-CLEA (R)), has been successfully demonstrated for the first time in C-C bond formation processes such as aldol, Henry and Mannich reactions. On the other hand, the Bayllis-Hillman reaction between 4-nitrobenzaldehyde and methyl vinyl ketone occurred through unspecific catalysis. Interestingly, aza-Michael addition reactions of secondary amines (diethylamine, piperidine and pyrrolidine) to acrylonitrile have been also efficiently catalyzed, observing with diethylamine the most remarkable differences between the enzyme-mediated reaction and the one in the absence of catalyst. Higher reactivities were attained with pyrrolidine demonstrating the versatility of hydrolases in organic synthesis. 
Bacillus licheniformis; C-C bond formation; C-N bond formation; enzyme catalysis; enzyme promiscuity