Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA)
Abstract Background The emergence of serious issues of multidrug resistance in the past few years have enforced the use of bacteriocins for combating infections. Threat posed to public health by various multidrug resistant (MDR) organisms can be resolved by discovering new antimicrobial proteins wit...
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doaj-f25213af664e441fb3cc9ae6da8ffd912020-11-25T01:34:56ZengBMCBMC Microbiology1471-21802018-11-0118111010.1186/s12866-018-1337-yScreening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA)Asma Ansari0Rashida Rahmat Zohra1Omer Mukhtar Tarar2Shah Ali Ul Qader3Afsheen Aman4The Karachi Institute of Biotechnology & Genetic Engineering (KIBGE)University of KarachiJinnah University for WomenFood and Marine Resources Research Centre, Pakistan Council of Scientific & Industrial Research (PCSIR), Laboratories Complex KarachiDepartment of Biochemistry, University of KarachiThe Karachi Institute of Biotechnology & Genetic Engineering (KIBGE)University of KarachiAbstract Background The emergence of serious issues of multidrug resistance in the past few years have enforced the use of bacteriocins for combating infections. Threat posed to public health by various multidrug resistant (MDR) organisms can be resolved by discovering new antimicrobial proteins with broad spectrum of inhibition. Results In the current study, Bacteriocin (BAC-IB17) produced by Bacillus subtilis KIBGE-IB17 is found to be effective against different strains of methicillin resistant Staphylococcus aureus (MRSA). The approximate molecular mass of BAC-IB17 is 10.7 kDa. This unique bacteriocin is found to be highly thermostable and pH stable in nature. It also showed its stability against various heavy metals, organic solvents, surfactants and proteolytic enzymes. Amino acid profile of BAC-IB17 clearly showed that this protein mainly consists of non-polar and basic amino acids whereas; some acidic amino acids were also detected. Sequence of first 15 amino acid residues obtained from N-terminal sequencing of BAC-IB17 were NKPEALVDYTGVXNS. Conclusions The anti-MRSA property of purified bacteriocin may be used to prevent the spread of MRSA infections. Remarkable features of BAC-IB17 suggests its applications in various pharmaceutical and food industries as it can function under a variety of harsh environmental conditions.http://link.springer.com/article/10.1186/s12866-018-1337-yAntibacterial potentialBacillus subtilisBacteriocin purificationMultidrug resistanceThermostable |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Asma Ansari Rashida Rahmat Zohra Omer Mukhtar Tarar Shah Ali Ul Qader Afsheen Aman |
spellingShingle |
Asma Ansari Rashida Rahmat Zohra Omer Mukhtar Tarar Shah Ali Ul Qader Afsheen Aman Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) BMC Microbiology Antibacterial potential Bacillus subtilis Bacteriocin purification Multidrug resistance Thermostable |
author_facet |
Asma Ansari Rashida Rahmat Zohra Omer Mukhtar Tarar Shah Ali Ul Qader Afsheen Aman |
author_sort |
Asma Ansari |
title |
Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) |
title_short |
Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) |
title_full |
Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) |
title_fullStr |
Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) |
title_full_unstemmed |
Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA) |
title_sort |
screening, purification and characterization of thermostable, protease resistant bacteriocin active against methicillin resistant staphylococcus aureus (mrsa) |
publisher |
BMC |
series |
BMC Microbiology |
issn |
1471-2180 |
publishDate |
2018-11-01 |
description |
Abstract Background The emergence of serious issues of multidrug resistance in the past few years have enforced the use of bacteriocins for combating infections. Threat posed to public health by various multidrug resistant (MDR) organisms can be resolved by discovering new antimicrobial proteins with broad spectrum of inhibition. Results In the current study, Bacteriocin (BAC-IB17) produced by Bacillus subtilis KIBGE-IB17 is found to be effective against different strains of methicillin resistant Staphylococcus aureus (MRSA). The approximate molecular mass of BAC-IB17 is 10.7 kDa. This unique bacteriocin is found to be highly thermostable and pH stable in nature. It also showed its stability against various heavy metals, organic solvents, surfactants and proteolytic enzymes. Amino acid profile of BAC-IB17 clearly showed that this protein mainly consists of non-polar and basic amino acids whereas; some acidic amino acids were also detected. Sequence of first 15 amino acid residues obtained from N-terminal sequencing of BAC-IB17 were NKPEALVDYTGVXNS. Conclusions The anti-MRSA property of purified bacteriocin may be used to prevent the spread of MRSA infections. Remarkable features of BAC-IB17 suggests its applications in various pharmaceutical and food industries as it can function under a variety of harsh environmental conditions. |
topic |
Antibacterial potential Bacillus subtilis Bacteriocin purification Multidrug resistance Thermostable |
url |
http://link.springer.com/article/10.1186/s12866-018-1337-y |
work_keys_str_mv |
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