Zinc-based organophyllosilicate nanosheets as novel carbonic anhydrase-like nanozyme for efficient CO2 fixation

Liu, Jin; Sun, Shiyong; Lv, Rui; Lin, Sen; Golubev, Yevgeny A.; Wang, Ke; Cao, Rui; Zeng, Yifan

doi:10.1016/j.seppur.2024.128979

Separation and Purification Technology

2025

DOI: 10.1016/j.seppur.2024.128979

|View full text |Cite

Zinc-based organophyllosilicate nanosheets as novel carbonic anhydrase-like nanozyme for efficient CO2 fixation

Jin Liu,

Shiyong Sun,

Rui Lv

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Carbon Dots with Polycyclic Dipeptide Structure Surpass Natural Hydrolase Performance

Zhang,

Wu,

Zhang

et al. 2024

Adv Funct Materials

View full text Add to dashboard Cite

Nature enzymes always suffer from high costs, harsh conditions, and instability, while, artificial one offers possibilities for addressing current challenges and plays a significant role in future industrial production. Here, the carbon dots (CDs), with well‐defined polycyclic dipeptide structures, are reported to exhibit superior hydrolase‐like catalytic performance beyond those of natural enzymes. Compared to natural lipase, the obtained CDs not only exhibit superior catalytic activity (2.85 times increase in Vm) but also have a broader range of substrate concentrations (0–8.0 mm) and substrate types (fatty ester, aromatic ester, phosphate ester), along with simpler catalytic conditions and superior stability. The highly efficient catalytic activity of CDs is attributed to the low activation energy of the reaction (Ea: 13.74 kJ mol−1) and strong adsorption to the substrates. The results of theoretical calculations and comparative experiments demonstrate that the adsorption sites of CDs are located on the nitrogen atoms of the polycyclic dipeptide. Furthermore, a membrane integrated with CDs (membrane‐catalyst) is constructed, through which the instantaneous hydrolysis of esters can be realized. This work provides new insight into the enzyme‐like catalytic mechanisms of CDs and offers a new approach to designing enzyme‐like materials with high performance.

show abstract

Carbon Dots with Polycyclic Dipeptide Structure Surpass Natural Hydrolase Performance

Zhang,

Wu,

Zhang

et al. 2024

Adv Funct Materials

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Zinc-based organophyllosilicate nanosheets as novel carbonic anhydrase-like nanozyme for efficient CO2 fixation

Cited by 1 publication

References 54 publications

Carbon Dots with Polycyclic Dipeptide Structure Surpass Natural Hydrolase Performance

Carbon Dots with Polycyclic Dipeptide Structure Surpass Natural Hydrolase Performance

Contact Info

Product

Resources

About