Cheng_2021_Enzyme.Microb.Technol_154_109962

Reference

Title : Synthesis of highly active enzyme-metal nanohybrids and uncovering the design rules - Cheng_2021_Enzyme.Microb.Technol_154_109962
Author(s) : Cheng G , Wu Q , Jiang C
Ref : Enzyme Microb Technol , 154 :109962 , 2021
Abstract :

Nanobiohybrid CAL-B/MNPs were synthesized through enzyme in situ reduction of metal ions, including noble and non-noble metals. Lipase CAL-B acted as multifunctional reagents (reducing and supporting agents). The hybrid catalysts were systematically characterized by HRTEM, EDX, MALDI-TOF-MS, and XPS analysis, confirming that highly dispersed 3-5 nm nanoparticles were evenly dispersed on lipase matrix without agglomeration. The mechanism of CAL-B reducing metal ions was investigated, revealing that AGLFFSSKDL in the amino acid sequence of CAL-B from 111 to 128 formed a stable spatial structure through hydrogen bonding, which was the key factor for enzyme in situ reduction of metal ions into highly dispersed nanoparticles.

PubMedSearch : Cheng_2021_Enzyme.Microb.Technol_154_109962
PubMedID: 34915246

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Citations formats

Cheng G, Wu Q, Jiang C (2021)
Synthesis of highly active enzyme-metal nanohybrids and uncovering the design rules
Enzyme Microb Technol 154 :109962

Cheng G, Wu Q, Jiang C (2021)
Enzyme Microb Technol 154 :109962