Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

The SGNH family esterases are highly effective biocatalysts due to their strong catalytic efficiencies, great stabilities, relatively small sizes, and ease of immobilization. Here, a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus NCFM, which has homologues in many Lactobacillus species, was identified, characterized, and immobilized. LaSGNH1 is highly active towards acetate- or butyrate-containing compounds, such as p-nitrophenyl acetate or 1-naphthyl acetate. Enzymatic properties of LaSGNH1, including thermal stability, optimum pH, chemical stability, and urea stability, were investigated. Interestingly, LaSGNH1 displayed a wide range of substrate specificity that included glyceryl tributyrate, tert-butyl acetate, and glucose pentaacetate. Furthermore, immobilization of LaSGNH1 by crosslinked enzyme aggregates (CLEAs) showed enhanced thermal stability and efficient recycling property. In summary, this work paves the way for molecular understandings and industrial applications of a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus.

Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity (PsEstA) from Paenibacillus sp.

Molecular information about family VIII esterases, which have similarities with class C β-lactamases and penicillin-binding proteins, remains largely unknown. In this study, a novel family VIII esterase with β-lactamase activity (PsEstA) from Paenibacillus sp. was characterized using several biochemical and biophysical methods. PsEstA was effective on a broad range of substrates including tertiary butyl acetate, glyceryl tributyrate, glucose pentaacetate, olive oil, and p-nitrophenyl esters. Additionally, PsEstA hydrolyzed nitrocefin, cefotaxime, and 7-aminocephalosporanic acid. Interestingly, two forms of immobilized PsEstA (CLEAs-PsEstA and mCLEAs-PsEstA) showed high recycling property and enhanced stability, but hybrid nanoflowers (hNFs) of PsEstA require improvement. This study provides a molecular understanding of substrate specificities, catalytic regulation, and immobilization of PsEstA, which can be efficiently used in biotechnological applications.

Imidazole Promoted Efficient Anomerization of β-D-Glucose Pentaacetate in Organic Solutions and Solid State

<p></p>Anomerization of glycosides were rarely performed under basic condition due to lack of efficiency. Here an imidazole promoted anomerization of β-D-glucose pentaacetate was developed; and reaction could proceed in both organic solvents and solid state at room temperature. Although mechanism is not yet clear, this unprecedent mild anomerization in solid state may open a new promising way for stereoseletive anomerization of broad glucosides and materials design in the future..

Imidazole Promoted Efficient Anomerization of β-D-Glucose Pentaacetate in Organic Solutions and Solid State

<p></p>Anomerization of glycosides were rarely performed under basic condition due to lack of efficiency. Here an imidazole promoted anomerization of β-D-glucose pentaacetate was developed; and reaction could proceed in both organic solvents and solid state at room temperature. Although mechanism is not yet clear, this unprecedent mild anomerization in solid state may open a new promising way for stereoseletive anomerization of broad glucosides and materials design in the future..

Imidazole Promoted Efficient Anomerization of β-D-Glucose Pentaacetate in Organic Solutions and Solid State

<p></p>Anomerization of glycosides were rarely performed under basic condition due to lack of efficiency. Here an imidazole promoted anomerization of β-D-glucose pentaacetate was developed; and reaction could proceed in both organic solvents and solid state at room temperature. Although mechanism is not yet clear, this unprecedent mild anomerization in solid state may open a new promising way for stereoseletive anomerization of broad glucosides and materials design in the future..

Imidazole Promoted Efficient Anomerization of β-D-Glucose Pentaacetate

Anomerization of glycosides were rarely performed under basic condition due to lack of efficiency. Here an imidazole promoted anomerization of β-D-glucose pentaacetate was developed; and the reaction was very efficient and full conversion could be achieved within an hour in several anhydrous solvents. Subsequently a new intramolecular mechanism was proposed based on investigation and following which anomerization of broad β-C(O)-O-glucosides might be expected in the future.

Extending the S-benzimidazolyl (SBiz) platform: N-alkylated SBiz glycosyl donors with the universal activation profile

This article describes the development of alkylated S-benzimidazolyl (SBiz) imidates as versatile building blocks for chemical glycosylation. The SBiz imidates have been originally developed as a new platform for active-latent glycosylations and its utility was further extended to other common strategies for oligosaccharide synthesis. This article expands upon the utility of these compounds. We developed a general protocol for the synthesis of a series of N-alkylated SBiz glycosides from N-protected SBiz aglycones by Lewis acid-mediated coupling with glucose pentaacetate. The N-alkylated SBiz moiety was found to be stable under strong basic conditions which allowed us to obtain both armed and disarmed N-alkylated SBiz donors. These donors showed good reactivity at a variety of activation conditions, and generally provided high yields in glycosylations.