PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24036201-0 2013 Enantiopure dihalocyclopropyl alcohols and esters by lipase catalyzed kinetic resolution. Esters 43-49 PAN0_003d1715 Moesziomyces antarcticus 53-59 31023008-0 2019 Stereodivergent Protein Engineering of a Lipase To Access All Possible Stereoisomers of Chiral Esters with Two Stereocenters. Esters 95-101 PAN0_003d1715 Moesziomyces antarcticus 41-47 28433899-4 2017 Finally, economically sustainable biofuel production was achieved providing high ester yield (<97%) along with augmented concentration (3.35M) in the reaction mixtures at relatively short esterification times, whereas the immobilized lipase maintained over 90% of its initial esterifying ability after reused for ten cycles. Esters 81-86 PAN0_003d1715 Moesziomyces antarcticus 237-243 28982086-6 2018 When NER@3DOM/m-OS was used repeatedly in batch reactions, the ester yields of n-butyl, octyl, and dodecyl levulinate could retain 46.18%, 82.33% and 81.25% after 9 reaction cycles, respectively, which was better than commercial lipase Novozym 435 under the same condition. Esters 63-68 PAN0_003d1715 Moesziomyces antarcticus 229-235 27534413-1 2017 The aim of this study was to develop simple and efficient method for immobilization of Candida antarctica lipase B onto hydrophobic anion exchange resin Purolite MN102 and to apply immobilized catalyst for the enzymatic synthesis of two valuable esters-isoamyl acetate and L-ascorbyl oleate. Esters 247-253 PAN0_003d1715 Moesziomyces antarcticus 106-112 17940805-0 2008 Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis. Esters 89-94 PAN0_003d1715 Moesziomyces antarcticus 66-72 21796287-4 2011 The assay applies p-nitrophenol octanoate (NPO) as the substrate and in the presence of lipase the ester is hydrolyzed to p-nitrophenolate which has a strong absorbance at 405 nm. Esters 99-104 PAN0_003d1715 Moesziomyces antarcticus 88-94 20017485-6 2010 In contrast, lipase B from Candida antarctica catalyzes the acylation of the phenolic group 4"-OH with 80% yield and negligible formation of higher esters. Esters 148-154 PAN0_003d1715 Moesziomyces antarcticus 13-19 15158806-4 2004 We propose that stampidine undergoes rapid enzymatic hydrolysis in the presence of lipase according to the following biochemical pathway: During the first step, hydrolysis of the ester group results in the formation of carboxylic acid. Esters 179-184 PAN0_003d1715 Moesziomyces antarcticus 83-89 18198845-2 2008 The lipase B from Candida antarctica was found to catalyze the cleavage of the ester bond in the HEMA end group of the formed polyesters, resulting in two major transesterification processes, methacrylate transfer and polyester transfer. Esters 79-84 PAN0_003d1715 Moesziomyces antarcticus 4-10 16356573-4 2006 The substrate concentration was 3.63-6.67 M in the eutectic media, whereas in organic media the concentration was below 0.10 M. Esters were synthesized with an immobilized Candida antarctica lipase, and optimum conditions were analyzed. Esters 128-134 PAN0_003d1715 Moesziomyces antarcticus 191-197 15158806-7 2004 We postulate that the lipase hydrolyzes the methyl ester group of the l-alanine side chain to form the cyclic intermediate in a stereoselective fashion. Esters 51-56 PAN0_003d1715 Moesziomyces antarcticus 22-28 15049361-3 2004 Among the various tested lipases, the one from Candida antarctica B gave the best results allowing 73% formation of the desired ester after 6 h. Comparing the efficiency of this latter lipase with the one of Amberlyst IR120H resin in catalyzing this reaction, the biocatalyst gave a molar yield of pyroglutamate lauroyl ester of 79% compared to 69% when using the ion exchange resin starting with 1.04 mmol substrate in each case. Esters 128-133 PAN0_003d1715 Moesziomyces antarcticus 25-31 11975561-4 2002 In contrast the lipase from Candida antarctica hydrolyzed the esters of trans-2-fluorocyclohexanol 2a and esterified the fluorohydrin itself with very low enantiopreference for the (R)-isomers. Esters 62-68 PAN0_003d1715 Moesziomyces antarcticus 16-22 11750885-4 2001 In contrast, a non-hyperbolic (sigmoidal) dependence of enzyme activity on ester concentration is found with human pancreatic lipase, triacylglycerol lipase from Humicola lanuginosa (Thermomyces lanuginosa) and partial acylglycerol lipase from Penicillium camembertii and the same substrates. Esters 75-80 PAN0_003d1715 Moesziomyces antarcticus 126-132 11750885-10 2001 It is assumed that the interaction of lipase with soluble multimolecular aggregates of tripropionin or short-chain vinyl esters or the formation of enzyme-substrate mixed micelles with ester bound to lipase, might represent a crucial step that triggers the structural transition to the open enzyme conformation by displacement of the lid. Esters 121-126 PAN0_003d1715 Moesziomyces antarcticus 38-44 11750885-10 2001 It is assumed that the interaction of lipase with soluble multimolecular aggregates of tripropionin or short-chain vinyl esters or the formation of enzyme-substrate mixed micelles with ester bound to lipase, might represent a crucial step that triggers the structural transition to the open enzyme conformation by displacement of the lid. Esters 121-126 PAN0_003d1715 Moesziomyces antarcticus 200-206 11180070-1 2001 Esters were prepared by acylation of hydroxypropyl cellulose with fatty acid catalyzed by immobilized lipase from Candida antarctica in tert-butanol. Esters 0-6 PAN0_003d1715 Moesziomyces antarcticus 102-108 10346941-1 1999 The oligosaccharide chain of the monodesmosidic haemolytic saponin digitonin (1) undergoes an efficient and regioselective acylation in organic solvent by use of Novozym 435 (lipase B from Candida antarctica supported on acrylic resin) in the presence of an activated ester. Esters 268-273 PAN0_003d1715 Moesziomyces antarcticus 175-181