Enzyme-catalysed siloxane bond formation

Bassindale, Alan R.; Brandstadt, Kurt F.; Lane, Thomas H.; Taylor, Peter G.

doi:10.1016/s0162-0134(03)00177-6

Cited by 56 publications

(60 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This is in agreement with the natural substrate-selectivity of the ROL, and suggests the involvement of the active site during the catalysis. Trypsin, a serine-protease that cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, was a good biocatalyst for trimethyloctyl silyl ether formation, and this is in line with our previous studies on the alkoxysilane hydrolysis and condensation reactions [7,9]. Lysozyme is a small (14.3 kDa) but robust protein consisting of a single 129 amino acid polypeptide chain , and it was already observed to be a good siloxane-bond biocatalyst [8].…”

Section: Methodssupporting

confidence: 81%

“…Our group has extensively studied silica precipitation [6] and the enzyme-catalyzed hydrolysis and condensation of alxokysilanes [7][8][9] under mild conditions. We have discovered several enzymatic candidates which were able to perform such reactions at room temperature and neutral pH and have investigated the potential involvement of their respective active sites in the biocatalyzed organo-silicon transformations.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme-Catalyzed Transetherification of Alkoxysilanes

et al. 2013

View full text Add to dashboard Cite

show abstract

Section: Methodssupporting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

Enzyme-Catalyzed Transetherification of Alkoxysilanes

et al. 2013

View full text Add to dashboard Cite

show abstract

“…[29] Lipases also catalyze Michael addition of various nucleophiles to 2-(trifluoromethyl)-propenoic acid. [30] Lipase [31] and trypsin [32] catalyze the condensation of silanols and alkoxysilanes, respectively, which involves formation of Si À O À Si bonds. Trypsin catalyzed the hydrolysis and condensation of trimethylethoxysilane to hexamethylsiloxane in water (Scheme 4).…”

Section: Catalytic Promiscuity Within the Same Proteinmentioning

confidence: 99%

Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways

2004

View full text Add to dashboard Cite

Biocatalysis has expanded rapidly in the last decades with the discoveries of highly stereoselective enzymes with broad substrate specificity. A new frontier for biocatalysis is broad reaction specificity, where enzymes catalyze alternate reactions. Although often under-appreciated, catalytic promiscuity has a natural role in evolution and occasionally in the biosynthesis of secondary metabolites. Examples of catalytic promiscuity with current or potential applications in synthesis are reviewed here. Combined with protein engineering, the catalytic promiscuity of enzymes may broadly extend their usefulness in organic synthesis.

show abstract

“…Zelisko et al have also used trypsin suspensions in dichloromethane, or from aqueous solutions, to facilitate the cross linking of α,ω-triethoxysilylethylpoly(dimethylsiloxane) [16,17]. While these experiments demonstrated that the trypsin-mediated cross-linking of silicone polymers was less efficient than the tin-mediated process at room temperature, when heat was added to the system, cross-linking was nearly complete after 24 h. Furthermore, reports in the literature have illustrated that trypsin, and to a lesser extent α-chymotrypsin, were capable of accelerating the rate of hexamethyldisiloxane formation from trimethylsilanol, as well as the hydrolysis and condensation of trimethylethoxysilane under buffered conditions [18]. Inhibition of the enzymes' active site led to almost complete recovery of starting materials.…”

Section: Introductionmentioning

confidence: 97%

Enzyme-mediated Synthesis of Silsesquioxanes

Frampton

Simionescu

Zelisko³

2009

Silicon

View full text Add to dashboard Cite

In an initial report we demonstrated that some serine proteases were suitable candidates for the hydrolysis and condensation of tetraethoxysilane and phenyltrimethoxysilane under solvent-free conditions. Using trypsin as a model enzyme, we have demonstrated the generality of this method by expanding the number of available silicon-based substrates that can be processed by the enzyme, as well as including pepsin to demonstrate that this phenomenon is not exclusive to a single family of enzymes. A series of time course 29 Si NMR experiments using D 2 O revealed that the rate of hydrolysis of phenyltrimethoxysilane could be enhanced by a factor of 11-155 times over enzyme-free controls when either trypsin or pepsin were used as catalysts. The following trend was observed when comparing the hydrolysis/condensation rates of a number of different organotrimethoxysilanes: methyltrimethoxysilane>allytrime-thoxysilane>ethyltrimethoxysilane>phenyltrimethoxysilane.

show abstract

Enzyme-catalysed siloxane bond formation

Cited by 56 publications

References 18 publications

Enzyme-Catalyzed Transetherification of Alkoxysilanes

Enzyme-Catalyzed Transetherification of Alkoxysilanes

Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways

Enzyme-mediated Synthesis of Silsesquioxanes

Contact Info

Product

Resources

About