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Enzymatic degradation of biofilm by metalloprotease from Microbacterium sp. SKS10

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Title Enzymatic degradation of biofilm by metalloprotease from Microbacterium sp. SKS10
 
Creator Saggu, Sandeep Kaur
Jha, Gopaljee
Mishra, Prakash Chandra
 
Subject alkaline protease
Microbacterium paraoxydans
metalloprotease
biofilm dispersal
staphylococcal biofilm
PROTEIN
PURIFICATION
ANTIGEN
 
Description Accepted date: 24 July 2019
Enzymes have replaced or decreased usage of toxic chemicals for industrial and medical applications leading toward sustainable chemistry. In this study, we report purification and characterization of a biofilm degrading protease secreted by Microbacterium sp. SKS10. The protease was identified as a metalloprotease, Peptidase M16 using mass spectrometry. It showed optimum activity at 60 degrees C, pH 12 and retained its activity in the presence of various salts and organic solvents. The enzyme was able to degrade biofilms efficiently at enzyme concentration lower than other known enzymes such as papain, trypsin and alpha-amylase. The presence of this protease increased the accessibility of antibiotics inside the biofilm, and was found to be non-cytotoxic toward human epidermoid carcinoma cells (A431) at the effective concentration for biofilm degradation. Thus, this protease may serve as an effective tool for management of biofilms.
SS is a UGC-MANF-SRF (University Grants CommissionMaulana Azad National Fellowship- Senior Research Fellow).
We would like to thank Dr. Rachna Hora, Assistant Professor,
Department of Molecular Biology and Biochemistry, Guru
Nanak Dev University, Amritsar, Punjab, India for reading
the manuscript. SS and PM were involved in the study design and wrote the
manuscript. SS carried out the experiments. GJ was involved in
mass spectrometry studies. All authors have read and approved
the final manuscript.
 
Date 2019-08-20T11:07:28Z
2019-08-20T11:07:28Z
2019
 
Type Article
 
Identifier Frontiers in Bioengineering and Biotechnology, 7: 192
2296-4185
http://223.31.159.10:8080/jspui/handle/123456789/972
https://www.frontiersin.org/articles/10.3389/fbioe.2019.00192/full
https://doi.org/10.3389/fbioe.2019.00192
 
Language en_US
 
Format application/pdf
 
Publisher Frontiers Media S.A.