Next Article in Journal
Influence of Indole-3-Acetic Acid and Gibberellic Acid on Phenylpropanoid Accumulation in Common Buckwheat (Fagopyrum esculentum Moench) Sprouts
Next Article in Special Issue
Special Issue: Enzyme Immobilization 2016
Previous Article in Journal
Peripheral and Cerebral Resistance Arteries in the Spontaneously Hypertensive Heart Failure Rat: Effects of Stilbenoid Polyphenols
Previous Article in Special Issue
Immobilized Trienzymatic System with Enhanced Stabilization for the Biotransformation of Lactose
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Molecules 2017, 22(3), 377;

Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes

Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China
Informalization Center for Education and Management, Jilin Agricultural University, Changchun 130118, China
College of Life Science, Jilin Agricultural University, Changchun 130118, China
Authors to whom correspondence should be addressed.
Academic Editor: Roberto Fernandez-Lafuente
Received: 15 January 2017 / Revised: 24 February 2017 / Accepted: 25 February 2017 / Published: 28 February 2017
(This article belongs to the Special Issue Enzyme Immobilization 2016)
Full-Text   |   PDF [9298 KB, uploaded 28 February 2017]   |  


β-galactosidase was successfully encapsulated within an amino-functionalised silica matrix using a “fish-in-net” approach and molecular imprinting technique followed by covalent binding of lysozyme via a glutaraldehyde-based method. Transmission electron microscopy (TEM), X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) spectroscopy were used to characterise the silica matrix hosting the two enzymes. Both encapsulated β-galactosidase and bound lysozyme exhibited high enzymatic activities and outstanding operational stability in model reactions. Moreover, enzyme activities of the co-immobilised enzymes did not obviously change relative to enzymes immobilised separately. In antibacterial tests, bound lysozyme exhibited 95.5% and 89.6% growth inhibition of Staphylococcus aureus ATCC (American type culture collection) 653 and Escherichia coli ATCC 1122, respectively. In milk treated with co-immobilised enzymes, favourable results were obtained regarding reduction of cell viability and high lactose hydrolysis rate. In addition, when both co-immobilised enzymes were employed to treat milk, high operational and storage stabilities were observed. The results demonstrate that the use of co-immobilised enzymes holds promise as an industrial strategy for producing low lactose milk to benefit people with lactose intolerance. View Full-Text
Keywords: β-galactosidase; lysozyme; encapsulation; covalent binding β-galactosidase; lysozyme; encapsulation; covalent binding

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Li, H.; Li, S.; Tian, P.; Wu, Z.; Li, Z. Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes. Molecules 2017, 22, 377.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top