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Influence of nanoparticle diameter on conjugated enzyme activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
19140 43045 2013 7 PDF Available
Title
Influence of nanoparticle diameter on conjugated enzyme activity
Abstract

•Lactase was covalently conjugated to magnetic particles of 18 nm, 50 nm, and 200 nm diameters.•Enzyme activity retention was inversely proportional to particle diameter.•kcat′ decreased with increasing particle size while Km′ was not significantly altered.•Loss of activity is attributed to enzyme-material surface interactions.

Lactase conjugated to nanomaterials represents an area of significant potential to the food processing as a means to produce novel value-added products, reduce waste, and enable diagnostics. While it is recognized that, in general, matter exhibits unique properties when manipulated at the nanoscale, little is known about how reducing the size of the carrier to the nanoscale effects attached lactase. The purpose of this work is to investigate the influence of particle size on activity retention of lactase (Aspergillus oryzae) covalently conjugated to magnetic nanoparticles of varying sizes. Lactase was attached to carboxylic acid functionalized magnetic nanoparticles 18 nm, 50 nm, and 200 nm in diameter using carbodiimide chemistry. After attachment, activity retention was 73%, 39%, and 14% compared to the free enzyme for the 18 nm, 50 nm, and 200 nm conjugates, respectively. The apparent Km was not significantly different as a function of particle size while the apparent kcat decreased with increasing particle size. Reducing the particle size of magnetic nanoparticles can increase the activity retention of conjugated lactase. This work provides improved understanding of enzyme-nanoparticles systems and allows for enhanced design of lactase-conjugated materials.

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Keywords
Galactosidase; Lactase; Nanoparticle; Nanomaterial; Bioprocessing; Immobilized enzyme
First Page Preview
Influence of nanoparticle diameter on conjugated enzyme activity
Publisher
Database: Elsevier - ScienceDirect
Journal: Food and Bioproducts Processing - Volume 91, Issue 4, October 2013, Pages 693–699
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering