Probing New Physics through mu-e Universality in K->lnu

The recent NA48/2 improvement on R_K=Gamma(K->e nu_e)/Gamma(K->mu nu_mu) emphasizes the role of K_l2 decays in probing the mu-e universality. Supersymmetric (SUSY) extensions of the Standard Model can exhibit mu-e non-universal contributions. Their origin is twofold: those deriving from lepton flavor conserving couplings are subdominant with respect to those arising from lepton flavor violating (LFV) sources. We show that mu-e non-universality in K_l2 is quite effective in constraining relevant regions of SUSY models with LFV (for instance, supergravities with a see-saw mechanism for neutrino masses). A comparison with analogous bounds coming from tau LFV decays proves the relevance of the measurement of R_K to probe LFV in SUSY.Comment: v2: 5 pages, 1 figure. Comments and 2 references adde

Perspectives on flow biocatalysis: the engine propelling enzymatic reactions

Flow biocatalysis has emerged as an empowering tool to boost the potential of enzymatic reactions towards more automatized, sustainable, and generally efficient synthetic processes. In the last fifteen years, the increasing number of biocatalytic transformations carried out in continuous flow exemplified the benefits that this technology can bring to incorporate biocatalysis into industrial operations. This perspective aims to capture in a nutshell the available methodologies for flow biocatalysis as well as to discuss the current limitations and the future directions in this field

A novel thymidine phosphorylase to synthesize (halogenated) anticancer and antiviral nucleoside drugs in continuous flow

Four pharmaceutically relevant nucleoside analogues (5-fluoro-2’-deoxyuridine, 5-chloro-2’-deoxyuridine, 5-bromo-2’-deoxyuridine, and 5-iodo-2’-deoxyuridine) have been synthesized by using a novel thymidine phosphorylase from H. elongata (HeTP). Following enzyme immobilization on microbeads, the biocatalyst was implemented as a packed-bed reactor for the continuous production of halogenated nucleosides, achieving up to 90% conversion at the 10 mM scale with 30 min residence time. Taking the synthesis of Floxuridine (5-fluoro-2’-deoxyuridine) as study case, we obtained the highest space-time yield (5.5 g/L/h) reported to date. In addition, bioinformatic tools such as MD analysis and CapiPy have contributed to shine light on the catalytic performance of HeTP as well as its immobilization, respectively

Spheroplasts preparation boosts the catalytic potential of a squalene-hopene cyclase

Squalene-hopene cyclases (SHCs) are a highly valuable and attractive class of membrane-bound enzymes as sustainable biotechnological tools to produce aromas and bioactive compounds at industrial scale. However, their application as whole-cell biocatalysts suffer from the outer cell membrane acting as a diffusion barrier for the highly hydrophobic substrate/product, while the use of purified enzymes leads to dramatic loss of stability. Here we present an unexplored strategy for biocatalysis: the application of SHC spheroplasts. By removing the outer cell membrane, we produced stable and substrate-accessible biocatalysts. SHC spheroplasts exhibited up to 100-fold higher activity than their whole-cell counterparts for the biotransformations of squalene, geranyl acetone, farnesol, and farnesyl acetone. Their catalytic ability was also higher than the purified enzyme for all high molecular weight terpenes. In addition, we introduce a new concept for the carrier-free immobilization of spheroplasts via crosslinking, CLS (crosslinked spheroplasts). The CLS maintained the same catalytic activity of the spheroplasts, offering additional advantages such as recycling and reuse. These timely solutions contribute not only to harness the catalytic potential of the SHCs, but also to make biocatalytic processes even greener and more cost-efficient

Use of Foundry Sands in the Production of Ceramic and Geopolymers for Sustainable Construction Materials

The aim of this research was to evaluate the possibility of reusing waste foundry sands derived from the production of cast iron as a secondary raw material for the production of building materials obtained both by high-temperature (ceramic tiles and bricks) and room-temperature (binders such as geopolymers) consolidation. This approach can reduce the current demand for quarry sand and/or aluminosilicate precursors from the construction materials industries. Samples for porcelain stoneware and bricks were produced, replacing the standard sand contained in the mixtures with waste foundry sand in percentages of 10%, 50%, and 100% by weight. For geopolymers, the sand was used as a substitution for metakaolin (30, 50, 70 wt%) as an aluminosilicate precursor rather than as an aggregate to obtain geopolymer pastes. Ceramic samples obtained using waste foundry sand were characterized by tests for linear shrinkage, water absorption, and colorimetry. Geopolymers formulations, produced with a Si/Al ratio of 1.8 and Na/Al = 1, were characterized to evaluate their chemical stability through measurements of pH and ionic conductivity, integrity in water, compressive strength, and microstructural analysis. The results show that the addition of foundry sand up to 50% did not significantly affect the chemical-physical properties of the ceramic materials. However, for geopolymers, acceptable levels of chemical stability and mechanical strength were only achieved when using samples made with 30% foundry sand as a replacement for metakaolin

Novel triple mutant of an extremophilic glycosyl hydrolase enables the rapid synthesis of thioglycosides

In order to expand the toolbox of enzymes available for thioglycoside synthesis, we describe here the first example of an extremophilic glycosyl hydrolase from Halothermothrix orenii (HorGH1) engineered towards thioglycosynthase activity with a novel combination of mutations. Using the triple mutant, HorGH1 M299R/E166A/E354G, a range of thioglycosides from glycosyl fluoride donors and aromatic thiols could be synthesised with exquisite stereoselectivity and good to excellent conversions (61-93%)

Dual Valorization of Lignin as a Versatile and Renewable Matrix for Enzyme Immobilization and (Flow) Bioprocess Engineering

Lignin has emerged as an attractive alternative in the search for more eco-friendly and less costly materials for enzyme immobi- lization. In this work, the terephthalic aldehyde-stabilization of lignin is carried out during its extraction to develop a series of functionalized lignins with a range of reactive groups (epoxy, amine, aldehyde, metal chelates). This expands the immobiliza- tion to a pool of enzymes (carboxylase, dehydrogenase, trans- aminase) by different binding chemistries, affording immobiliza- tion yields of 64–100%. As a proof of concept, a ω- transaminase reversibly immobilized on polyethyleneimine- lignin is integrated in a packed-bed reactor. The stability of the immobilized biocatalyst is tested in continuous-flow deamina- tion reactions and maintains the same conversion for 100 cycles. These results outperform previous stability tests carried out with the enzyme covalently immobilized on methacrylic resins, with the advantage that the reversibility of the immobilized enzyme allows recycling and reuse of lignin beyond the enzyme inactivation. Additionally, an in-line system also based on lignin is added into the downstream process to separate the reaction products by catch-and-release. These results demonstrate a fully closed-loop sustainable flow- biocatalytic system based exclusively on lignin