Immobilization of enzymes on alumina by means of pyridoxal 5′-phosphate

1988 ◽  
Vol 8 (3) ◽  
pp. 263-269 ◽  
Author(s):  
M. Pugnière ◽  
C. San Juan ◽  
M-A. Coletti-Previero ◽  
A. Previero

A number of proteases have been immobilized on alumina in a two-step procedure: the first step converted them into semisynthetic phosphoproteins which, in the second step, spontaneously bonded to alumina through their phosphate function. The immobilized enzymes thus obtained showed the physical properties typical of the inorganic carrier and a high activity on low molecular weight substrates.

Catalysts ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 195 ◽  
Author(s):  
Ivan Bernar ◽  
Floris Rutjes ◽  
Johannes Elemans ◽  
Roeland Nolte

We report on the highly efficient epoxidation of low-molecular-weight and polymeric olefins catalyzed by a supramolecular manganese porphyrin complex using molecular oxygen as an oxidant and an aldehyde as a co-reductant. At ambient temperature and under optimized reaction conditions, the catalyst showed high activity and stereoselectivity. The efficiency of the supramolecular manganese porphyrin was higher than that of a reference porphyrin catalyst, possibly because it was more stable under the applied reaction conditions. Mechanistic studies suggest that a manganese oxo porphyrin complex may be an intermediate in the epoxidation reaction.


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