Immobilization of EreB on Acid-Modified Palygorskite for Highly Efficient Degradation of Erythromycin

Int J Environ Res Public Health. 2022 Sep 4;19(17):11064. doi: 10.3390/ijerph191711064.

Abstract

Erythromycin is one of the most commonly used macrolide antibiotics. However, its pollution of the ecosystem is a significant risk to human health worldwide. Currently, there are no effective and environmentally friendly methods to resolve this issue. Although erythromycin esterase B (EreB) specifically degrades erythromycin, its non-recyclability and fragility limit the large-scale application of this enzyme. In this work, palygorskite was selected as a carrier for enzyme immobilization. The enzyme was attached to palygorskite via a crosslinking reaction to construct an effective erythromycin-degradation material (i.e., EreB@modified palygorskite), which was characterized using FT-IR, SEM, XRD, and Brunauer-Emmett-Teller techniques. The results suggested the successful modification of the material and the loading of the enzyme. The immobilized enzyme had a higher stability over varying temperatures (25-65 °C) and pH values (6.5-10.0) than the free enzyme, and the maximum rate of reaction (Vmax) and the turnover number (kcat) of the enzyme increased to 0.01 mM min-1 and 169 min-1, respectively, according to the enzyme-kinetics measurements. The EreB@modified palygorskite maintained about 45% of its activity after 10 cycles, and degraded erythromycin in polluted water to 20 mg L-1 within 300 min. These results indicate that EreB could serve as an effective immobilizing carrier for erythromycin degradation at the industrial scale.

Keywords: EreB; erythromycin degradation; immobilization; palygorskite.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carboxylic Ester Hydrolases* / chemistry
  • Ecosystem
  • Enzymes, Immobilized*
  • Erythromycin* / chemistry
  • Humans
  • Hydrogen-Ion Concentration
  • Magnesium Compounds / chemistry
  • Silicon Compounds / chemistry
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Enzymes, Immobilized
  • Magnesium Compounds
  • Silicon Compounds
  • Erythromycin
  • Carboxylic Ester Hydrolases
  • erythromycin esterase
  • attapulgite

Grants and funding

This study was financially supported by Yili Chuanning Biotechnology Co., Ltd. (2019K1238 and 2019K1237); Jiangsu Bi’ao Environmental Technology Co., Ltd. China; General Project No.175 of the Guizhou Science and Technology Support Program.