Microencapsulation of Gulosibacter molinativorax ON4 cells by a spray-drying process using different biopolymers.

J Hazard Mater

LEPABE, Departamento de Engenharia Química, Faculdade de Engenharia da Universidade do Porto, Rua Dr. Roberto Frias, 4200-465 Porto, Portugal.

Published: September 2017


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Molinate is a thiocarbamate herbicide used in rice crop protection. As other pesticides, molinate is a recognized environmental pollutant and bio-accumulated by some wildlife forms. Gulosibacter molinativorax ON4 is able to hydrolyse molinate into metabolites which are further degraded by other un-related bacteria. Hence, it can be used in molinate bioremediation processes. The aim of this work was to investigate the possibility of producing G. molinativorax ON4 microparticles, using different non-toxic biopolymers (arabic gum, modified chitosan, calcium alginate and sodium alginate) as encapsulating agents by a spray-drying process. Several formulations of microparticles were prepared, and their physicochemical structures were analyzed by scanning electron microscopy (SEM), laser granulometry analysis and zeta potential analysis. The obtained microparticles were evaluated considering their ability to degrade molinate, the metabolic activity (by colour development of the tetrazolium violet redox), and also the survival rate and shelf-life/storage stability of microparticles. Based on their molinate degrading activity, the biopolymers calcium alginate and modified chitosan cross-linked with tripolyphosphate appear to be the best options for the microencapsulation of the G. molinativorax ON4. However, the microparticles produced with modified chitosan cross-linked with tripolyphosphate present the best combination of physical properties and activity degradation of molinate.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.jhazmat.2017.05.018DOI Listing

Publication Analysis

Top Keywords

molinativorax on4
16
modified chitosan
12
gulosibacter molinativorax
8
spray-drying process
8
on4 microparticles
8
calcium alginate
8
chitosan cross-linked
8
cross-linked tripolyphosphate
8
molinate
7
microparticles
5

Similar Publications

In silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4.

Sci Rep

September 2022

LEPABE - Laboratory for Process Engineering, Environment, Biotechnology and Energy, Departamento de Engenharia Química, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, 4200-465, Porto, Portugal.

Gulosibacter molinativorax ON4 is the only known organism to produce molinate hydrolase (MolA), which catalyses the breakdown of the thiocarbamate herbicide into azepane-1-carboxylic acid (ACA) and ethanethiol. A combined genomic and transcriptomic strategy was used to fully characterize the strain ON4 genome, particularly the molA genetic environment, to identify the potential genes encoding ACA degradation enzymes. Genomic data revealed that molA is the only catabolic gene of a novel composite transposon (Tn6311), located in a novel low copy number plasmid (pARLON1) harbouring a putative T4SS of the class FATA.

View Article and Find Full Text PDF

Microencapsulation of Gulosibacter molinativorax ON4 cells by a spray-drying process using different biopolymers.

J Hazard Mater

September 2017

LEPABE, Departamento de Engenharia Química, Faculdade de Engenharia da Universidade do Porto, Rua Dr. Roberto Frias, 4200-465 Porto, Portugal.

Molinate is a thiocarbamate herbicide used in rice crop protection. As other pesticides, molinate is a recognized environmental pollutant and bio-accumulated by some wildlife forms. Gulosibacter molinativorax ON4 is able to hydrolyse molinate into metabolites which are further degraded by other un-related bacteria.

View Article and Find Full Text PDF

Microbial degradation of the herbicide molinate by defined cultures and in the environment.

Appl Microbiol Biotechnol

December 2013

LEPAE, Departamento Engenharia Química, Faculdade de Engenharia, Universidade do Porto, Rua Dr. Roberto Frias, 4200-465, Porto, Portugal,

Molinate is a thiocarbamate herbicide used worldwide in rice crop protection. As with other pesticides, molinate is a recognized environmental pollutant, detected in soils, irrigation water, or rivers and bio-accumulated by some wildlife forms. For this reason, and in spite of its low toxicity to humans, environmental protection measures, which include reduction of use and/or remediation processes, are recommended.

View Article and Find Full Text PDF

Molinate biodegradation in soils: natural attenuation versus bioaugmentation.

Appl Microbiol Biotechnol

March 2013

LEPAE, Departamento de Engenharia Química, Faculdade de Engenharia, Universidade do Porto, 4200-465 Porto, Portugal.

The aims of the present study were to assess the potential of natural attenuation or bioaugmentation to reduce soil molinate contamination in paddy field soils and the impact of these bioremediation strategies on the composition of soil indigenous microbiota. A molinate mineralizing culture (mixed culture DC) was used as inoculum in the bioaugmentation assays. Significantly higher removal of molinate was observed in bioaugmentation than in natural attenuation microcosms (63 and 39 %, respectively) after 42 days of incubation at 22 °C.

View Article and Find Full Text PDF

Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.

J Bacteriol

October 2011

LEPAE-Departamento de Engenharia Química, Faculdade de Engenharia, Universidade do Porto, Porto, Portugal.

A new pathway of molinate mineralization has recently been described. Among the five members of the mixed culture able to promote such a process, Gulosibacter molinativorax ON4(T) has been observed to promote the initial breakdown of the herbicide into ethanethiol and azepane-1-carboxylate. In the current study, the gene encoding the enzyme responsible for molinate hydrolysis was identified and heterologously expressed, and the resultant active protein was purified and characterized.

View Article and Find Full Text PDF