2639-63-6Relevant articles and documents
Solvent Configuration influences Enzyme Activity in Organic Media
Ottolina, Gianluca,Gianinetti, Francesca,Riva, Sergio,Carrea, Giacomo
, p. 535 - 536 (1994)
The activities of three hydrolases and one oxidoreductase have been found to be different when using (R)-carvone or (S)-carvone as the reaction medium indicating that solvent geometry can influence enzyme catalysis.
A chemically modified lipase preparation for catalyzing the transesterification reaction in even highly polar organic solvents
Solanki, Kusum,Gupta, Munishwar Nath
, p. 2934 - 2936 (2011)
Acylation of Pseudomonas cepacia lipase with Pyromellitic dianhydride to modify 72% of total amino groups was carried out. Different organic solvents were screened for precipitation of modified lipase. It was found that 1,2-dimethoxyethane was the best pr
Enzyme Access Tunnel Engineering in Baeyer-Villiger Monooxygenases to Improve Oxidative Stability and Biocatalyst Performance
Bornscheuer, Uwe,Kim, Myeong-Ju,Oh, Deok-Kun,Park, Jin-Byung,Park, Seongsoon,Park, So-Yeon,Seo, Eun-Ji
supporting information, (2021/11/10)
Hydrogen peroxide is involved in a variety of enzyme catalysis as an oxidant or toxic by-product. Thereby, attenuation of the H2O2-driven oxidative stress is one of the key issues for preparative biocatalysis. Here, a rational approach to improve the robustness of enzymes, in particular, Baeyer-Villiger monooxygenases (BVMOs) against H2O2 was investigated. The enzyme access tunnels, which may serve as exit paths for H2O2 from the active site to the bulk, were predicted by using the CAVER and/or protein energy landscape exploration (PELE) software for the phenylacetone monooxygenase variant (PAMO_C65D) from Thermobifida fusca and the BVMO from Pseudomonas putida KT2440. The amino acid residues, which are susceptible to oxidation by H2O2 (e. g., methionine and tyrosine) and located in vicinity of the predicted H2O2 migration paths, were substituted with less reactive or inert amino acids (e. g., leucine and isoleucine). This led to design of the H2O2-resistant enzyme variants, which became robust biocatalysts for synthetic applications. For instance, the H2O2-resistant P. putida BVMO reached turnover numbers of 4,100 for the BV oxygenation of 4-decanone, which is 2.8-fold greater than the parent enzyme. Moreover, the H2O2-resistant P. putida BVMO allowed 2-fold enhancement in titer of 9-(nonanoyloxy)nonanoic acid (8) formation in a cascade fatty acid biotransformation. Therefore, it was assumed that the CAVER/PELE-based H2O2 migration path engineering represents an efficient rational design approach to improve not only oxidative stability but also biotransformation performance of the H2O2-forming or utilizing enzymes (e. g., BVMOs, oxidases, and peroxidases). (Figure presented.).
Efficient Enzymatic Preparation of Flavor Esters in Water
Perdomo, Igor Chiarelli,Gianolio, Stefania,Pinto, Andrea,Romano, Diego,Contente, Martina Letizia,Paradisi, Francesca,Molinari, Francesco
, p. 6517 - 6522 (2019/06/20)
A straightforward biocatalytic method for the enzymatic preparation of different flavor esters starting from primary alcohols (e.g., isoamyl, n-hexyl, geranyl, cinnamyl, 2-phenethyl, and benzyl alcohols) and naturally available ethyl esters (e.g., formate, acetate, propionate, and butyrate) was developed. The biotransformations are catalyzed by an acyltransferase from Mycobacterium smegmatis (MsAcT) and proceeded with excellent yields (80-97%) and short reaction times (30-120 min), even when high substrate concentrations (up to 0.5 M) were used. This enzymatic strategy represents an efficient alternative to the application of lipases in organic solvents and a significant improvement compared with already known methods in terms of reduced use of organic solvents, paving the way to sustainable and efficient preparation of natural flavoring agents.
Graphite oxide as an efficient solid reagent for esterification reactions
Mirza-Aghayan, Maryam,Rahimifard, Mahshid,Boukherroub, Rabah
, p. 859 - 864 (2014/12/10)
Esterification of organic acids with alcohols under mild conditions in high yields using graphite oxide, a readily available and inexpensive material, as an effective reagent is described.