How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures

Bibliographic Details
Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Boros, Zoltán, Falus, Péter, Márkus, Mária, Weiser, Diána, Oláh, Márk, Hornyánszky, Gábor, Nagy, József, Poppe, László
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier BV 2013
Subjects:
Process Chemistry and Technology
Biochemistry
Bioengineering
Catalysis
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1016/j.molcatb.2012.09.004
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spelling crelsevierbv:10.1016/j.molcatb.2012.09.004 2023-10-01T03:51:33+02:00 How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures Boros, Zoltán Falus, Péter Márkus, Mária Weiser, Diána Oláh, Márk Hornyánszky, Gábor Nagy, József Poppe, László 2013 http://dx.doi.org/10.1016/j.molcatb.2012.09.004 https://api.elsevier.com/content/article/PII:S1381117712002561?httpAccept=text/xml https://api.elsevier.com/content/article/PII:S1381117712002561?httpAccept=text/plain en eng Elsevier BV https://www.elsevier.com/tdm/userlicense/1.0/ Journal of Molecular Catalysis B: Enzymatic volume 85-86, page 119-125 ISSN 1381-1177 Process Chemistry and Technology Biochemistry Bioengineering Catalysis journal-article 2013 crelsevierbv https://doi.org/10.1016/j.molcatb.2012.09.004 2023-09-01T00:05:39Z Article in Journal/Newspaper Antarc* Antarctica ScienceDirect (Elsevier - via Crossref) Journal of Molecular Catalysis B: Enzymatic 85-86 119 125
institution Open Polar
collection ScienceDirect (Elsevier - via Crossref)
op_collection_id crelsevierbv
language English
topic Process Chemistry and Technology
Biochemistry
Bioengineering
Catalysis
spellingShingle Process Chemistry and Technology
Biochemistry
Bioengineering
Catalysis
Boros, Zoltán
Falus, Péter
Márkus, Mária
Weiser, Diána
Oláh, Márk
Hornyánszky, Gábor
Nagy, József
Poppe, László
How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
topic_facet Process Chemistry and Technology
Biochemistry
Bioengineering
Catalysis
format Article in Journal/Newspaper
author Boros, Zoltán
Falus, Péter
Márkus, Mária
Weiser, Diána
Oláh, Márk
Hornyánszky, Gábor
Nagy, József
Poppe, László
author_facet Boros, Zoltán
Falus, Péter
Márkus, Mária
Weiser, Diána
Oláh, Márk
Hornyánszky, Gábor
Nagy, József
Poppe, László
author_sort Boros, Zoltán
title How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
title_short How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
title_full How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
title_fullStr How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
title_full_unstemmed How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
title_sort how the mode of candida antarctica lipase b immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
publisher Elsevier BV
publishDate 2013
url http://dx.doi.org/10.1016/j.molcatb.2012.09.004
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https://api.elsevier.com/content/article/PII:S1381117712002561?httpAccept=text/plain
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Journal of Molecular Catalysis B: Enzymatic
volume 85-86, page 119-125
ISSN 1381-1177
op_rights https://www.elsevier.com/tdm/userlicense/1.0/
op_doi https://doi.org/10.1016/j.molcatb.2012.09.004
container_title Journal of Molecular Catalysis B: Enzymatic
container_volume 85-86
container_start_page 119
op_container_end_page 125
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