Zobrazeno 1 - 10
of 287
pro vyhledávání: '"Sergio Riva"'
Publikováno v:
Catalysts, Vol 13, Iss 5, p 819 (2023)
The enzymatic acetylation in the organic solvents of a number of the important bioactive cardiac glycosides was investigated. With the bufanolide proscillaridin A and the cardenolide lanatoside C, acylation, as expected, occurred at the secondary 4
Externí odkaz:
https://doaj.org/article/e06ef263b1914b96b18d649a1a182ee6
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 4, p 3524 (2023)
The bio-oxidation of a series of aromatic amines catalyzed by T. versicolor laccase has been investigated exploiting either commercially available nitrogenous substrates [(E)-4-vinyl aniline and diphenyl amine] or ad hoc synthetized ones [(E)-4-styry
Externí odkaz:
https://doaj.org/article/aebd94e9b3104f3997ec796dfbe734ac
Autor:
Erica Elisa Ferrandi, Ivan Bassanini, Susanna Bertuletti, Sergio Riva, Chiara Tognoli, Marta Vanoni, Daniela Monti
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 20, p 12153 (2022)
In a metagenome mining-based search of novel thermostable hydroxysteroid dehydrogenases (HSDHs), enzymes that are able to selectively oxidize/reduce steroidal compounds, a novel short-chain dehydrogenase/reductase (SDR), named Is2-SDR, was recently d
Externí odkaz:
https://doaj.org/article/76bec9339af348d6b8fda7fb9281d4e1
Autor:
Michele Crotti, Fabio Parmeggiani, Erica Elisa Ferrandi, Francesco G. Gatti, Alessandro Sacchetti, Sergio Riva, Elisabetta Brenna, Daniela Monti
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 7 (2019)
Ene reductases from the Old Yellow Enzyme (OYE) family are industrially interesting enzymes for the biocatalytic asymmetric reduction of alkenes. To access both enantiomers of the target reduced products, stereocomplementary pairs of OYE enzymes are
Externí odkaz:
https://doaj.org/article/ca9d1cb7d59445678eb55e6236f26ce6
Publikováno v:
Catalysts, Vol 11, Iss 1, p 26 (2020)
Laccases are multicopper oxidases, which have been widely investigated in recent decades thanks to their ability to oxidize organic substrates to the corresponding radicals while producing water at the expense of molecular oxygen. Besides their succe
Externí odkaz:
https://doaj.org/article/0b67ee7215f14b0998dcd3025aaab3ce
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 11, Iss 1, Pp 1583-1595 (2015)
Dicarboxylic acids and their derivatives (esters and anhydrides) have been used as acylating agents in lipase-catalyzed reactions in organic solvents. The synthetic outcomes have been dimeric or hybrid derivatives of bioactive natural compounds as we
Externí odkaz:
https://doaj.org/article/fd9740ba02014ead984fb42ed32a952e
Autor:
Eva Vavříková, Paolo Gavezzotti, Kateřina Purchartová, Kateřina Fuksová, David Biedermann, Marek Kuzma, Sergio Riva, Vladimír Křen
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 11983-11995 (2015)
A panel of lipases was screened for the selective acetylation and alcoholysis of silychristin and silychristin peracetate, respectively. Acetylation at primary alcoholic group (C-22) of silychristin was accomplished by lipase PS (Pseudomonas cepacia)
Externí odkaz:
https://doaj.org/article/166024512956455a8591b2c81b745748
Autor:
Sergio Riva, Wolf-Dieter Fessner
This ready reference presents environmentally friendly and stereoselective methods of modern biocatalysis. The experienced and renowned team of editors have gathered top international authors for this book. They cover such emerging topics as chemoenz
Autor:
Erica Elisa Ferrandi, Ivan Bassanini, Giovanni Fronza, Sergio Riva, Daniela Monti, Susanna Bertuletti
Publikováno v:
ChemCatChem
(2021). doi:10.1002/cctc.202101307
info:cnr-pdr/source/autori:Bertuletti S.; Ferrandi E.E.; Monti D.; Fronza G.; Bassanini I.; Riva S./titolo:Synthesis of ?-Muricholic Acid by One-Pot Enzymatic Mitsunobu Inversion using Hydroxysteroid Dehydrogenases/doi:10.1002%2Fcctc.202101307/rivista:ChemCatChem (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume
(2021). doi:10.1002/cctc.202101307
info:cnr-pdr/source/autori:Bertuletti S.; Ferrandi E.E.; Monti D.; Fronza G.; Bassanini I.; Riva S./titolo:Synthesis of ?-Muricholic Acid by One-Pot Enzymatic Mitsunobu Inversion using Hydroxysteroid Dehydrogenases/doi:10.1002%2Fcctc.202101307/rivista:ChemCatChem (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume
The biocatalyzed conversion of hyocholic acid (3?,6?,7?-trihydroxy-5?-cholan-24-oic acid) into ?-muricholic acid (3?,6?,7?-trihydroxy-5?-cholan-24-oic acid) has been obtained exploiting a small library of 7?- and 7?-HSDHs (hydroxysteroid dehydrogenas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f591d3b4a4c9179cf3f06f4b0d620a0
https://doi.org/10.1002/cctc.202101307
https://doi.org/10.1002/cctc.202101307
Autor:
Sergio Riva, Erica Elisa Ferrandi, Ivan Bassanini, Daniela Monti, Ikram Bayout, Nassima Bouzemi, Susanna Bertuletti
Publikováno v:
European journal of organic chemistry (Online) (2021). doi:10.1002/ejoc.202100174
info:cnr-pdr/source/autori:Bertuletti S.; Bayout I.; Bassanini I.; Ferrandi E.E.; Bouzemi N.; Monti D.; Riva S./titolo:Biocatalytic Approaches to the Enantiomers of Wieland-Miescher Ketone and its Derivatives/doi:10.1002%2Fejoc.202100174/rivista:European journal of organic chemistry (Online)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Bertuletti S.; Bayout I.; Bassanini I.; Ferrandi E.E.; Bouzemi N.; Monti D.; Riva S./titolo:Biocatalytic Approaches to the Enantiomers of Wieland-Miescher Ketone and its Derivatives/doi:10.1002%2Fejoc.202100174/rivista:European journal of organic chemistry (Online)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume
Biocatalytic approaches have been investigated in order to isolate the enantiomers of Wieland-Miescher ketone (1) and of its alcoholic derivatives (cis-2 and trans-3). Specifically, two enzymes from our in-house metagenomic collection of oxidoreducta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::595922d908d3a812822051cd389c210c
https://doi.org/10.1002/ejoc.202100174
https://doi.org/10.1002/ejoc.202100174