WFRF:(Clausen Ib Groth)
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 04634naa a2200817 4500 | |
| 001 | oai:DiVA.org:kth-74874 | |
| 003 | SwePub | |
| 008 | 120203s1993 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-748742 URI |
| 024 | 7 | a https://doi.org/10.1007/BF010249332 DOI |
| 040 | a (SwePub)kth | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Holmquist, Mats Torstenu KTH,Biokemi och biokemisk teknologi4 aut0 (Swepub:kth)u11ohkl7 |
| 245 | 1 0 | a Lipases from Rhizomucor miehei and Humicola lanuginosa :b Modification of the lid covering the active site alters enantioselectivity |
| 264 | 1 | c 1993 |
| 338 | a print2 rdacarrier | |
| 500 | a Chemicals/CAS: 1,2-cyclohexanedione, 765-87-7; Arginine, 74-79-3; Cyclohexanones; Decanoates; Enzymes, Immobilized; Lipase, EC 3.1.1.3; Phenylglyoxal, 1074-12-0 NR 20140805QC 20180614 | |
| 520 | a The homologous lipases from Rhizomucor miehei and Humicola lanuginosa showed approximately the same enantioselectivity when 2-methyldecanoic acid esters were used as substrates. Both lipases preferentially hydrolyzed the S- enantiomer of 1-heptyl 2-methyldecanoate (R. miehei: E(S) = 8.5; H. lanuginosa: E(S) = 10.5), but the R-enantiomer of phenyl 2-methyldecanoate (E(R) = 2.9). Chemical arginine specific modification of the R. miehei lipase with 1,2-cyclohexanedione resulted in a decreased enantioselectivity (E(R) = 2.0), only when the phenyl ester was used as a substrate. In contrast, treatment with phenylglyoxal showed a decreased enantioselectivity (E(S) = 2.5) only when the heptyl ester was used as a substrate. The presence of guanidine, an arginine side chain analog, decreased the enantioselectivity with the heptyl ester (E(S) = 1.9) and increased the enantioselectivity with the aromatic ester (E(R) = 4.4) as substrates. The mutation, Glu 87 Ala, in the lid of the H. lanuginosa lipase, which might decrease the electrostatic stabilization of the open-lid conformation of the lipase, resulted in 47% activity compared to the native lipase, in a tributyrin assay. The Glu 87 Ala mutant showed an increased enantioselectivity with the heptyl ester (E(S) = 17.4) and a decreased enantioselectivity with the phenyl ester (E(R) = 2.5) as substrates, compared to native lipase. The enantioselectivities of both lipases in the esterification of 2-methyldecanoic acid with 1-heptanol were unaffected by the lid modifications. | |
| 650 | 7 | a NATURVETENSKAPx Kemix Organisk kemi0 (SwePub)104052 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciencesx Organic Chemistry0 (SwePub)104052 hsv//eng |
| 653 | a alanine | |
| 653 | a arginine | |
| 653 | a decanoic acid derivative | |
| 653 | a ester | |
| 653 | a guanidine | |
| 653 | a heptanol | |
| 653 | a phenylglyoxal | |
| 653 | a triacylglycerol lipase | |
| 653 | a article | |
| 653 | a chemical modification | |
| 653 | a enantiomer | |
| 653 | a enzyme activation | |
| 653 | a enzyme active site | |
| 653 | a enzyme conformation | |
| 653 | a enzyme substrate | |
| 653 | a esterification | |
| 653 | a gas chromatography | |
| 653 | a hydrolysis | |
| 653 | a lipid metabolism | |
| 653 | a nonhuman | |
| 653 | a site directed mutagenesis | |
| 653 | a Comparative Study | |
| 653 | a Cyclohexanones | |
| 653 | a Decanoates | |
| 653 | a Enzymes | |
| 653 | a Immobilized | |
| 653 | a Kinetics | |
| 653 | a Lipase | |
| 653 | a Mitosporic Fungi | |
| 653 | a Mucorales | |
| 653 | a Stereoisomerism | |
| 653 | a Substrate Specificity | |
| 653 | a Support | |
| 653 | a Non-U.S. Gov't | |
| 653 | a Humicola | |
| 653 | a Rhizomucor miehei | |
| 653 | a Thermomyces lanuginosus | |
| 700 | 1 | a Martinelle, Matsu KTH,Industriell bioteknologi4 aut0 (Swepub:kth)u1yqglux |
| 700 | 1 | a Berglund, P.u Mid Sweden University4 aut0 (Swepub:kth)u1271chh |
| 700 | 1 | a Clausen, Ib Grothu Novo-Nordisk A/S, Bagsvaerd, Denmark4 aut |
| 700 | 1 | a Patkar, Shamkant4 aut |
| 700 | 1 | a Svendsen, Allanu Novo-Nordisk A/S, Bagsvaerd, Denmark4 aut |
| 700 | 1 | a Hult, Karlu KTH,Biokemi och biokemisk teknologi4 aut0 (Swepub:kth)u1nzlwuj |
| 710 | 2 | a KTHb Biokemi och biokemisk teknologi4 org |
| 773 | 0 | t Journal of Protein Chemistryg 12:6, s. 749-757q 12:6<749-757x 0277-8033 |
| 856 | 4 | u http://www.scopus.com/inward/record.url?eid=2-s2.0-0027730414&partnerID=40&md5=de0921e2eeb500bbe4371128d80deef3 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-74874 |
| 856 | 4 8 | u https://doi.org/10.1007/BF01024933 |
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