Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.

Conventional leather processing involving depilation of animal hide by lime and sulphide treatment generates considerable amounts of chemical waste causing severe environmental pollution. Enzymatic depilation is an environmentally friendly process and has been considered to be a viable alternative t...

Full description

Bibliographic Details
Main Authors: Emmanuel Vijay Paul Pandeeti, Gopi Krishna Pitchika, Jyotsna Jotshi, Smita S Nilegaonkar, Pradnya P Kanekar, Dayananda Siddavattam
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3037957?pdf=render
id doaj-c9227e39ca5e47b494c970ee9c65c937
record_format Article
spelling doaj-c9227e39ca5e47b494c970ee9c65c9372020-11-25T00:11:44ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0162e1674210.1371/journal.pone.0016742Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.Emmanuel Vijay Paul PandeetiGopi Krishna PitchikaJyotsna JotshiSmita S NilegaonkarPradnya P KanekarDayananda SiddavattamConventional leather processing involving depilation of animal hide by lime and sulphide treatment generates considerable amounts of chemical waste causing severe environmental pollution. Enzymatic depilation is an environmentally friendly process and has been considered to be a viable alternative to the chemical depilation process. We isolated an extracellular protease from Pseudomonas aeruginosa strain MCM B-327 with high depilation activity using buffalo hide as a substrate. This 33 kDa protease generated a peptide mass fingerprint and de novo sequence that matched perfectly with LasB (elastase), of Pseudomonas aeruginosa. In support of this data a lasB mutant of MCM B-327 strain lacked depilatory activity and failed to produce LasB. LasB heterologously over-produced and purified from Escherichia coli also exhibited high depilating activity. Moreover, reintroduction of the lasB gene to the P. aeruginosa lasB mutant via a knock-in strategy also successfully restored depilation activity thus confirming the role of LasB as the depilating enzyme.http://europepmc.org/articles/PMC3037957?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Emmanuel Vijay Paul Pandeeti
Gopi Krishna Pitchika
Jyotsna Jotshi
Smita S Nilegaonkar
Pradnya P Kanekar
Dayananda Siddavattam
spellingShingle Emmanuel Vijay Paul Pandeeti
Gopi Krishna Pitchika
Jyotsna Jotshi
Smita S Nilegaonkar
Pradnya P Kanekar
Dayananda Siddavattam
Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
PLoS ONE
author_facet Emmanuel Vijay Paul Pandeeti
Gopi Krishna Pitchika
Jyotsna Jotshi
Smita S Nilegaonkar
Pradnya P Kanekar
Dayananda Siddavattam
author_sort Emmanuel Vijay Paul Pandeeti
title Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
title_short Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
title_full Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
title_fullStr Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
title_full_unstemmed Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
title_sort enzymatic depilation of animal hide: identification of elastase (lasb) from pseudomonas aeruginosa mcm b-327 as a depilating protease.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2011-01-01
description Conventional leather processing involving depilation of animal hide by lime and sulphide treatment generates considerable amounts of chemical waste causing severe environmental pollution. Enzymatic depilation is an environmentally friendly process and has been considered to be a viable alternative to the chemical depilation process. We isolated an extracellular protease from Pseudomonas aeruginosa strain MCM B-327 with high depilation activity using buffalo hide as a substrate. This 33 kDa protease generated a peptide mass fingerprint and de novo sequence that matched perfectly with LasB (elastase), of Pseudomonas aeruginosa. In support of this data a lasB mutant of MCM B-327 strain lacked depilatory activity and failed to produce LasB. LasB heterologously over-produced and purified from Escherichia coli also exhibited high depilating activity. Moreover, reintroduction of the lasB gene to the P. aeruginosa lasB mutant via a knock-in strategy also successfully restored depilation activity thus confirming the role of LasB as the depilating enzyme.
url http://europepmc.org/articles/PMC3037957?pdf=render
work_keys_str_mv AT emmanuelvijaypaulpandeeti enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
AT gopikrishnapitchika enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
AT jyotsnajotshi enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
AT smitasnilegaonkar enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
AT pradnyapkanekar enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
AT dayanandasiddavattam enzymaticdepilationofanimalhideidentificationofelastaselasbfrompseudomonasaeruginosamcmb327asadepilatingprotease
_version_ 1725402492034875392