Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica

Horino, Satoshi; Wagner, Karla; Hummel, Anke; Kanomata, Kyohei; Gröger, Harald; Akai, Shuji

doi:https://doi.org/10.1002/ejoc.202400242

Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica

Horino, Satoshi; Wagner, Karla; Hummel, Anke et al.

European Journal of Organic Chemistry, 2024, 27(21), e202400242

Number of Access:563（2025-08-17 22:19 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/96482

Link to primary information

File	Format	Terms of use	Size	Views	Date.Available	Description	information
EurJOrgChem_27_21_e202400242	pdf	None	5.43 MB	138	2025.06.03

Item Information

Output File Export EndNote Basic Export Mendeley

Title	Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica
Creator	CreatorName Horino, Satoshi
	CreatorName Wagner, Karla
	CreatorName Hummel, Anke
	NRID 1000030880447 1000030880447 ORCID 0000-0002-2251-4665 0000-0002-2251-4665 researchmap permalink kyohei_kanomata kyohei_kanomata Scopus Author ID 39861733600 39861733600 CreatorName Kanomata, Kyohei
	CreatorName Gröger, Harald
	NRID 1000060192457 1000060192457 researchmap permalink shuji_akai shuji_akai Scopus Author ID 7006001526 7006001526 ORCID 0000-0001-9149-8745 0000-0001-9149-8745 CreatorName Akai, Shuji
Subject	kinetic resolution
	lipase
	tertiary alcohol
Description	This is the peer reviewed version of the following article: Horino S., Wagner K., Hummel A., et al. Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica. European Journal of Organic Chemistry 27, e202400242 (2024), which has been published in final form at https://doi.org/10.1002/ejoc.202400242. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
Abstract	Enzyme-catalyzed acylative kinetic resolution (KR) and dynamic kinetic resolution (DKR) of racemic primary and secondary alcohols have been widely reported to produce esters with high enantiomeric purity. In contrast, similar KRs of tertiary alcohols have been reported for only a limited range of substrates and require prolonged reaction times of several days. To gain deeper insight into the substrate scope and increase the process efficiency, we examined the reaction conditions using commercially available immobilized lipase A from Candida antarctica and found that the addition of the heterogeneous, inorganic base sodium carbonate significantly increased the reaction rate while maintaining high enantioselectivity. The use of vinyl hexanoate as the acyl donor provided esters that were stable during chromatography purification. The optimized reaction conditions were then successfully applied to a range of cyclic tertiary alcohols containing tetralin, dihydroindene, chromane, and thiochromane skeletons having, in part, a substituent on the aromatic ring. In this study on the structure–reactivity relationship of enzymatic KR-type reactions, we achieved >30 % conversion for various tertiary alcohols in 24 h at 25 °C, producing optically active esters with 88–99 % ee.
Publisher	John Wiley and Sons Inc
Source Title	European Journal of Organic Chemistry
Volume (Issue)	27(21)
Page	e202400242
Date of Issued	2024-06-03
Language	English
Handle URL	https://hdl.handle.net/11094/96482
PISSN	1434193X
eISSN	10990690
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1002/ejoc.202400242
Access Rights	open access
CopyRight	© 2024 Wiley-VCH GmbH.
oaire:version	Accepted Manuscript
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCTERMS.bibliographicCitation	European Journal of Organic Chemistry. 2024, 27(21), p. e202400242
DC.title	Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica
DC.creator	Horino, Satoshi
	Wagner, Karla
	Hummel, Anke
	Kanomata, Kyohei
	Gröger, Harald
	Akai, Shuji
DC.publisher	John Wiley and Sons Inc
DC.language' scheme='DCTERMS.RFC1766	English
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2024-06-03
DC.identifier	https://doi.org/10.1002/ejoc.202400242
DC.subject	kinetic resolution
	lipase
	tertiary alcohol
DC.description	This is the peer reviewed version of the following article: Horino S., Wagner K., Hummel A., et al. Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica. European Journal of Organic Chemistry 27, e202400242 (2024), which has been published in final form at https://doi.org/10.1002/ejoc.202400242. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
DCTERMS.abstract	Enzyme-catalyzed acylative kinetic resolution (KR) and dynamic kinetic resolution (DKR) of racemic primary and secondary alcohols have been widely reported to produce esters with high enantiomeric purity. In contrast, similar KRs of tertiary alcohols have been reported for only a limited range of substrates and require prolonged reaction times of several days. To gain deeper insight into the substrate scope and increase the process efficiency, we examined the reaction conditions using commercially available immobilized lipase A from Candida antarctica and found that the addition of the heterogeneous, inorganic base sodium carbonate significantly increased the reaction rate while maintaining high enantioselectivity. The use of vinyl hexanoate as the acyl donor provided esters that were stable during chromatography purification. The optimized reaction conditions were then successfully applied to a range of cyclic tertiary alcohols containing tetralin, dihydroindene, chromane, and thiochromane skeletons having, in part, a substituent on the aromatic ring. In this study on the structure–reactivity relationship of enzymatic KR-type reactions, we achieved >30 % conversion for various tertiary alcohols in 24 h at 25 °C, producing optically active esters with 88–99 % ee.
DC.rights	© 2024 Wiley-VCH GmbH.
DC.format	96482
citation_title	Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica
citation_author	Horino, Satoshi
	Wagner, Karla
	Hummel, Anke
	Kanomata, Kyohei
	Gröger, Harald
	Akai, Shuji
citation_publisher	John Wiley and Sons Inc
citation_language	English
citation_date	2024-06-03
citation_journal_title	European Journal of Organic Chemistry
citation_volume	27
citation_issue	21
citation_firstpage	e202400242
citation_doi	https://doi.org/10.1002/ejoc.202400242
citation_public_url	https://hdl.handle.net/11094/96482

Kinetic Resolution of Cyclic Tertiary Alcohols with Lipase A from Candida Antarctica

Link to primary information

Item Information

Show details