Enhancement of photo-driven biomethanation under visible light by nano-engineering of Rhodopseudomonas palustris.

Biomethanation is of great interest as it can transform CO to methane under ambient conditions. In particular, genetically engineered bacterium of Rhodopseudomonas palustris showed great promise for one-step biomethanation powered by solar energy, which is attractive for CO fixation as well as solar energy storage. However, biomethanation with R.

Characterization of EstZY: A new acetylesterase with 7-aminocephalosporanic acid deacetylase activity from Alicyclobacillus tengchongensis.

Deacetyl-7-aminocephalosporanic acid (D-7-ACA) is required for producing of many semisynthetic β-lactam antibiotics; therefore, enzymes capable of converting 7-aminocephalosporanic acid (7-ACA) to D-7-ACA present a valuable resource to the pharmaceutical industry. In the present study, a putative acetylesterase, EstZY, was identified and characterized from a thermophilic bacterium Alicyclobacillus tengchongensis. Sequence alignment showed that EstZY was an acetylesterase which belonged to carbohydrate esterase family 7 (CE7), with substrate preference for short-chain acyl esters p-NPC to p-NPC.

Identification and characterization of an acetyl esterase from Paenibacillus sp. XW-6-66 and its novel function in 7-aminocephalosporanic acid deacetylation.

Objectives: To obtain a new acetyl esterase from Paenibacillus sp. XW-6-66 and apply the enzyme to 7-aminocephalosporanic acid (7-ACA) deacetylation.

Results: The acetyl esterase AesZY was identified from Paenibacillus sp.

A thermostable and alkaline GDSL-motif esterase from Bacillus sp. K91: crystallization and X-ray crystallographic analysis.

The esterase Est8 from the thermophilic bacterium Bacillus sp. K91 belongs to the GDSL family and is active on a variety of acetylated compounds, including 7-aminocephalosporanic acid. In contrast to other esterases of the GDSL family, the catalytic residues Asp182 and His185 were more pivotal for the catalytic activity of Est8 than the Ser11 residue.