Preparation of enzyme nanoparticles and studying the catalytic activity of the immobilized nanoparticles on polyethylene films

David Meridor; Aharon Gedanken

doi:10.1016/j.ultsonch.2012.06.005

Preparation of enzyme nanoparticles and studying the catalytic activity of the immobilized nanoparticles on polyethylene films

David Meridor
, Aharon Gedanken

Department of Chemistry

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

Using high-intensity ultrasound, in situ generated α-amylase nanoparticles (NPs) were immobilized on polyethylene (PE) films. The α-amylase NP-coated PE films have been characterized by E-SEM, FTIR, DLS, XPS and RBS. The PE was reacted with HNO₃ and NPs of the α-amylase were also deposited on the activated PE. The PE impregnated with α-amylase (4 μg per 1 mg PE) was used for hydrolyzing soluble potato starch to maltose. The immobilization improved the catalytic activity of α-amylase at all the reaction conditions studied. The kinetic parameters, K_m (5 and 4 g L^-1 for the regular and activated PE, respectively) and V_max (5 × 10^-7 mol ml^-1 min^-1, almost the same numbers were obtained for the regular and activated PEs) for the immobilized amylase were found to slightly favor the respective values obtained for the free enzyme (K_m = 6.6 g L ^-1, V_max = 3.7 × 10^-7 mol ml^-1 min^-1). The enzyme remained bound to PE even after soaking the PE in a starch solution for 72 h and was still found to be weakly active.

Original language	English
Pages (from-to)	425-431
Number of pages	7
Journal	Ultrasonics Sonochemistry
Volume	20
Issue number	1
DOIs	https://doi.org/10.1016/j.ultsonch.2012.06.005
State	Published - Jan 2013

Bibliographical note

Funding Information:
YL is grateful to the funding support from Natural Science Foundation of China ( 51476155 , 51127002 ), National Basic Research Program of China (973 Program) (2013CB834602), Anhui Provincial Natural Science Foundation ( 1408085J09 ), Fundamental Research Funds for the Central Universities (WK2320000020) and Chinese Academy of Sciences. PD acknowledges support from the European Research Council under the European Community's Seventh Framework Programme (FP7/2007–2013)/ERC Grant agreement no. 291049 – 2G-CSafe . The technical assistance from Dr. Jiuzhong Yang, Dr. Zhanjun Cheng and Mr. Yizun Wang is also appreciated.

Funding

YL is grateful to the funding support from Natural Science Foundation of China ( 51476155 , 51127002 ), National Basic Research Program of China (973 Program) (2013CB834602), Anhui Provincial Natural Science Foundation ( 1408085J09 ), Fundamental Research Funds for the Central Universities (WK2320000020) and Chinese Academy of Sciences. PD acknowledges support from the European Research Council under the European Community's Seventh Framework Programme (FP7/2007–2013)/ERC Grant agreement no. 291049 – 2G-CSafe . The technical assistance from Dr. Jiuzhong Yang, Dr. Zhanjun Cheng and Mr. Yizun Wang is also appreciated.

Funders	Funder number
FP7/2007
European Commission	291049
National Natural Science Foundation of China	51476155, 51127002
Chinese Academy of Sciences
Natural Science Foundation of Anhui Province	1408085J09
Seventh Framework Programme
National Basic Research Program of China (973 Program)	2013CB834602
Fundamental Research Funds for the Central Universities	WK2320000020

Keywords

Amylase
Enzyme
Nanoparticles
Sonochemical coatings

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10.1016/j.ultsonch.2012.06.005

Cite this

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title = "Preparation of enzyme nanoparticles and studying the catalytic activity of the immobilized nanoparticles on polyethylene films",

abstract = "Using high-intensity ultrasound, in situ generated α-amylase nanoparticles (NPs) were immobilized on polyethylene (PE) films. The α-amylase NP-coated PE films have been characterized by E-SEM, FTIR, DLS, XPS and RBS. The PE was reacted with HNO3 and NPs of the α-amylase were also deposited on the activated PE. The PE impregnated with α-amylase (4 μg per 1 mg PE) was used for hydrolyzing soluble potato starch to maltose. The immobilization improved the catalytic activity of α-amylase at all the reaction conditions studied. The kinetic parameters, Km (5 and 4 g L-1 for the regular and activated PE, respectively) and Vmax (5 × 10-7 mol ml-1 min-1, almost the same numbers were obtained for the regular and activated PEs) for the immobilized amylase were found to slightly favor the respective values obtained for the free enzyme (Km = 6.6 g L -1, Vmax = 3.7 × 10-7 mol ml-1 min-1). The enzyme remained bound to PE even after soaking the PE in a starch solution for 72 h and was still found to be weakly active.",

keywords = "Amylase, Enzyme, Nanoparticles, Sonochemical coatings",

author = "David Meridor and Aharon Gedanken",

note = "Funding Information: YL is grateful to the funding support from Natural Science Foundation of China ( 51476155 , 51127002 ), National Basic Research Program of China (973 Program) (2013CB834602), Anhui Provincial Natural Science Foundation ( 1408085J09 ), Fundamental Research Funds for the Central Universities (WK2320000020) and Chinese Academy of Sciences. PD acknowledges support from the European Research Council under the European Community's Seventh Framework Programme (FP7/2007–2013)/ERC Grant agreement no. 291049 – 2G-CSafe . The technical assistance from Dr. Jiuzhong Yang, Dr. Zhanjun Cheng and Mr. Yizun Wang is also appreciated. ",

year = "2013",

month = jan,

doi = "10.1016/j.ultsonch.2012.06.005",

language = "אנגלית",

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AU - Meridor, David

AU - Gedanken, Aharon

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AB - Using high-intensity ultrasound, in situ generated α-amylase nanoparticles (NPs) were immobilized on polyethylene (PE) films. The α-amylase NP-coated PE films have been characterized by E-SEM, FTIR, DLS, XPS and RBS. The PE was reacted with HNO3 and NPs of the α-amylase were also deposited on the activated PE. The PE impregnated with α-amylase (4 μg per 1 mg PE) was used for hydrolyzing soluble potato starch to maltose. The immobilization improved the catalytic activity of α-amylase at all the reaction conditions studied. The kinetic parameters, Km (5 and 4 g L-1 for the regular and activated PE, respectively) and Vmax (5 × 10-7 mol ml-1 min-1, almost the same numbers were obtained for the regular and activated PEs) for the immobilized amylase were found to slightly favor the respective values obtained for the free enzyme (Km = 6.6 g L -1, Vmax = 3.7 × 10-7 mol ml-1 min-1). The enzyme remained bound to PE even after soaking the PE in a starch solution for 72 h and was still found to be weakly active.

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Preparation of enzyme nanoparticles and studying the catalytic activity of the immobilized nanoparticles on polyethylene films

Abstract

Bibliographical note

Funding

Keywords

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