Enzymatic Degradation of Biofilm by Metalloprotease From Microbacterium sp. SKS10.

Sandeep Kaur Saggu,Prakash Chandra Mishra,Gopaljee Jha

doi:10.3389/fbioe.2019.00192

Abstract

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°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 α-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.

Highlights

Biofilms are a city of microbes (Watnick and Kolter, 2000) that adhere to each other forming complex tertiary structures that stick to a surface (Lopez et al, 2010)
An alkaline protease producing bacterial strain was isolated from soil of west coast region of India
This study extrapolates the potential of an extracellular protease secreted by Microbacterium sp

Summary

Introduction

Biofilms are a city of microbes (Watnick and Kolter, 2000) that adhere to each other forming complex tertiary structures that stick to a surface (Lopez et al, 2010). The cells in biofilms have the capability to mutate and exchange genetic information helping them to survive in severe growth conditions (Singh et al, 2017). They are provided with various benefits such as physical defense from the host immune system and antimicrobials, sorption and storage of nutrients, tolerance to desiccation, and synchronization of virulence factor expression through quorum sensing. The main component of the S. aureus biofilm matrix is polysaccharide intercellular adhesin composed of β-1,6-linkedN-acetylglucosamine polymer and many proteins such as protein A, fibrinogen-binding proteins, clumping factor B etc. The main component of the S. aureus biofilm matrix is polysaccharide intercellular adhesin composed of β-1,6-linkedN-acetylglucosamine polymer and many proteins such as protein A, fibrinogen-binding proteins, clumping factor B etc. (Lister and Horswill, 2014)

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