@article{3067916,
    title = "Enzymatic removal of carboxyl protecting groups. 2. Cleavage of the benzyl and methyl moieties",
    author = "Barbayianni, E. and Fotakopoulou, I. and Schmidt, M. and Constantinou-Kokotou, V. and Bornscheuer, U.T. and Kokotos, G.",
    journal = "The Journal of Organic Chemistry",
    year = "2005",
    volume = "70",
    number = "22",
    pages = "8730-8733",
    doi = "10.1021/jo051004v",
    keywords = "Bacteria;  Benzene;  Carboxylation;  Esterification, Bacillus subtilis (BS2);  Functional groups;  Moieties;  Selective removal, Enzymes, amino acid;  bacterial enzyme;  benzyl derivative;  carboxylic acid;  ester;  esterase;  fungal enzyme;  methyl group;  peptide;  phospholipase A2 inhibitor;  recombinant enzyme;  triacylglycerol lipase, article;  Bacillus subtilis;  Candida antarctica;  carbon nuclear magnetic resonance;  chemical reaction;  chemical structure;  enzyme activity;  enzyme inhibition;  Escherichia coli;  hydrolysis;  nonhuman;  proton nuclear magnetic resonance, Bacillus subtilis;  Benzene;  Candida;  Esters;  Hydrolysis;  Lipase;  Methylation;  Molecular Structure;  Pancreatic Elastase;  Peptides;  Phospholipases A",
    abstract = "Enzymes are versatile reagents for the efficient removal of methyl and benzyl protecting groups. An esterase from Bacillus subtilis (BS2) and a lipase from Candida antarctica (CAL-A) allow a mild and selective removal of these moieties in high yields without affecting other functional groups. © 2005 American Chemical Society."
}