Bernard Henrissat

Bernard Henrissat

Bernard Henrissat


University of Grenoble, France

+33 (0)4 13 94 95 12

Scientific Publications




About The Scientist

Short Biography

Bernard Henrissat obtained a Ph.D. in Chemistry in 1979 (University of Grenoble, France) and a D.Sc. in Physical Sciences in 1985 (University of Grenoble, France). After a postdoc at the Xerox Research Centre of Canada, he did most of his career at CNRS (Grenoble, then Marseille, France) studying carbohydrate-active enzymes. In 2014 Bernard Henrissat was recruited by King Abdulaziz University at the Department of Biological Sciences. In 2015 he received the prestigious Novozymes Prize for his work on the classification of carbohydrate-active enzymes.

Current Research Interest :

    Carbohydrate-active enzymes (glycoside hydrolases, polysaccharide lyases, carbohydrate esterases, glycosyltransferases and associated auxiliary activities) in genomics and metagenomics for their role in health, nutrition and biotechnology.

Researcher ID:

Five Of The Most Important Publications

(1) Lapebie P, Lombard V, Drula E, Terrapon N, Henrissat B (2019) Bacteroidetes use thousands of enzyme combinations to break down glycans. Nature Communications, 10:2043.
(2) Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O’Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ (2017) Metabolism of a complex pectin reveals novel enzymatic adaptations in the human gut microbiota. Nature, 544:65-70.
(3) Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (2014) The Carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 42:D490-D495.
(4) El Kaoutari A, Armougom F, Gordon JI, Raoult D, Henrissat B (2013) The abundance and variety of carbohydrate-active enzymes in the human gut microbiota. Nature Reviews Microbiology, 11:497-504.
(5) Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.

Last Update
2/13/2023 2:19:20 PM