Encapsulation of CALB by nucleotide/metal ions coordination nanoparticles: highly selective catalysis of esterification while poor performance in glycerolysis reaction. (16th September 2021)
- Record Type:
- Journal Article
- Title:
- Encapsulation of CALB by nucleotide/metal ions coordination nanoparticles: highly selective catalysis of esterification while poor performance in glycerolysis reaction. (16th September 2021)
- Main Title:
- Encapsulation of CALB by nucleotide/metal ions coordination nanoparticles: highly selective catalysis of esterification while poor performance in glycerolysis reaction
- Authors:
- Chen, Wenyi
Xu, Li
Zhong, Nanjing - Abstract:
- Abstract: BACKGROUND: Enzymatic esterification is attracting for particular high‐acid oil deacidification. In this study, Candida antarctica lipase B (CALB) was encapsulated into a series of nucleotide‐hybrid metal coordination polymers (CPs), which were constructed by guanosine 5′‐monophosphate (GMP) and various metals. RESULTS: We here found that, most of the present CPs encapsulated CALB (CALB@CPs) samples were highly selective for esterification while poor in glycerolysis reaction. They exhibited quite poor performance in glycerolysis, with triacylglycerols (TAGs) conversion lower than 5%, despite this considerable enzymatic hydrolysis activities were observed. However, they (most of them) showed good performance in esterification of fatty acids and glycerol for TAG synthesis. In addition, the GMP/Tb (CPs constructed by GMP and Tb 3+ ) encapsulated CALB (CALB@GMP/Tb) transformed over 98% of oleic acid into glycerides in the high‐acid oil deacidification process, and TAG content from 87 to 89% was obtained. Moreover, the CALB@GMP/Tb showed good reusability in the esterification system. CONCLUSION: The present CALB@CPs samples are selective for esterification and suitable for high‐acid oils deacidification. This work provides a new system for enzymatic selectivity improvement study. © 2021 Society of Chemical Industry.
- Is Part Of:
- Journal of the science of food and agriculture. Volume 102:Number 5(2022)
- Journal:
- Journal of the science of food and agriculture
- Issue:
- Volume 102:Number 5(2022)
- Issue Display:
- Volume 102, Issue 5 (2022)
- Year:
- 2022
- Volume:
- 102
- Issue:
- 5
- Issue Sort Value:
- 2022-0102-0005-0000
- Page Start:
- 1812
- Page End:
- 1822
- Publication Date:
- 2021-09-16
- Subjects:
- Candida antarctica lipase B -- coordination polymers -- encapsulated enzyme -- esterification -- glycerolysis
Food -- Periodicals
Agriculture -- Periodicals
664 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jsfa.11516 ↗
- Languages:
- English
- ISSNs:
- 0022-5142
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5055.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 21090.xml