scispace - formally typeset
B

Benevides C. C. Pessela

Researcher at Spanish National Research Council

Publications -  92
Citations -  3563

Benevides C. C. Pessela is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Immobilized enzyme & Lipase. The author has an hindex of 30, co-authored 88 publications receiving 3253 citations. Previous affiliations of Benevides C. C. Pessela include Instituto Politécnico Nacional.

Papers
More filters
Journal ArticleDOI

Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins

TL;DR: Very active and highly stabilized derivatives of many enzymes and proteins have been prepared using activated supports that immobilize proteins, via a two-point reaction involving the region/s of the protein surface with the higher densities of amino groups.
Journal ArticleDOI

Epoxy-Amino Groups: A New Tool for Improved Immobilization of Proteins by the Epoxy Method

TL;DR: Stability of the immobilized enzyme has been found to be much higher using the new support than in preparations using the conventional ones in many cases, and immobilization is much more rapid using amino-epoxy supports than employing conventional epoxy supports.
Journal ArticleDOI

Advances in the design of new epoxy supports for enzyme immobilization-stabilization.

TL;DR: The possibilities of a directed immobilization of mutated enzymes (change of an amino acid by cysteine on specific points of the protein surface) on tailor-made disulfide-epoxy supports will be discussed as an almost-ideal procedure to achieve very intense and very efficient rigidification of a desired region of industrial enzymes.
Journal ArticleDOI

The immobilization of a thermophilic β-galactosidase on Sepabeads supports decreases product inhibition: Complete hydrolysis of lactose in dairy products

TL;DR: In this paper, the β-galactosidase from Thermus sp. T2 (Htag-BgaA) was shown to be competitively inhibited by galactose (3.1 mM) and non-competitively by glucose (49.9 mM).