An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive
A proteolytic strain of Bacillus pumilus MP 27 was isolated from water samples of Southern ocean produced alkaline protease. Since protease production need expensive ingredients, an economically viable process was developed by using low cost carbon source, wheat straw, supplemented with peptone. Thi...
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ftdoajarticles:oai:doaj.org/article:43dabd77725c4095bffd669515512db5 2023-05-15T18:25:37+02:00 An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive Mehak Baweja Rameshwar Tiwari Puneet Kumar Singh Lata Nain Pratyoosh Shukla 2016-08-01T00:00:00Z https://doi.org/10.3389/fmicb.2016.01195 https://doaj.org/article/43dabd77725c4095bffd669515512db5 EN eng Frontiers Media S.A. http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01195/full https://doaj.org/toc/1664-302X 1664-302X doi:10.3389/fmicb.2016.01195 https://doaj.org/article/43dabd77725c4095bffd669515512db5 Frontiers in Microbiology, Vol 7 (2016) Protease Docking Molecular modeling surfactant Bacillus pumilus De-staining Microbiology QR1-502 article 2016 ftdoajarticles https://doi.org/10.3389/fmicb.2016.01195 2022-12-31T14:58:34Z A proteolytic strain of Bacillus pumilus MP 27 was isolated from water samples of Southern ocean produced alkaline protease. Since protease production need expensive ingredients, an economically viable process was developed by using low cost carbon source, wheat straw, supplemented with peptone. This protease was active within temperature ranges 10˚C -70˚C at pH 9. This process was optimized by response surface methodology using a Box Bekhman design by Design Expert 7.0 software that increased the protease activity to 776.5 U/ml. Moreover, the enzyme was extremely stable at a broad range of temperature and pH retaining 69% of its activity at 50 ºC and 70% at pH 11. The enzyme exhibited excellent compatibility with surfactants and commercial detergents, showing 87% stability with triton X-100 and ̴ 100% stability with Tide commercial detergent. The results of the wash performance analysis demonstrated considerably good de-staining at 50ºC and 4ºC with low supplementation (109 U/ml). Molecular modeling of the protease revealed the presence of serine proteases, subtilase family and serine active site and further docking supported the association of catalytic site with the various substrates. Certainly, such protease can be considered as a good detergent additive in detergent industry with a possibility to remove the stains effectively even in a cold wash. Article in Journal/Newspaper Southern Ocean Directory of Open Access Journals: DOAJ Articles Southern Ocean Triton ENVELOPE(-55.615,-55.615,49.517,49.517) Frontiers in Microbiology 7 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Protease Docking Molecular modeling surfactant Bacillus pumilus De-staining Microbiology QR1-502 |
spellingShingle |
Protease Docking Molecular modeling surfactant Bacillus pumilus De-staining Microbiology QR1-502 Mehak Baweja Rameshwar Tiwari Puneet Kumar Singh Lata Nain Pratyoosh Shukla An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
topic_facet |
Protease Docking Molecular modeling surfactant Bacillus pumilus De-staining Microbiology QR1-502 |
description |
A proteolytic strain of Bacillus pumilus MP 27 was isolated from water samples of Southern ocean produced alkaline protease. Since protease production need expensive ingredients, an economically viable process was developed by using low cost carbon source, wheat straw, supplemented with peptone. This protease was active within temperature ranges 10˚C -70˚C at pH 9. This process was optimized by response surface methodology using a Box Bekhman design by Design Expert 7.0 software that increased the protease activity to 776.5 U/ml. Moreover, the enzyme was extremely stable at a broad range of temperature and pH retaining 69% of its activity at 50 ºC and 70% at pH 11. The enzyme exhibited excellent compatibility with surfactants and commercial detergents, showing 87% stability with triton X-100 and ̴ 100% stability with Tide commercial detergent. The results of the wash performance analysis demonstrated considerably good de-staining at 50ºC and 4ºC with low supplementation (109 U/ml). Molecular modeling of the protease revealed the presence of serine proteases, subtilase family and serine active site and further docking supported the association of catalytic site with the various substrates. Certainly, such protease can be considered as a good detergent additive in detergent industry with a possibility to remove the stains effectively even in a cold wash. |
format |
Article in Journal/Newspaper |
author |
Mehak Baweja Rameshwar Tiwari Puneet Kumar Singh Lata Nain Pratyoosh Shukla |
author_facet |
Mehak Baweja Rameshwar Tiwari Puneet Kumar Singh Lata Nain Pratyoosh Shukla |
author_sort |
Mehak Baweja |
title |
An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
title_short |
An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
title_full |
An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
title_fullStr |
An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
title_full_unstemmed |
An Alkaline Protease from Bacillus pumilus MP 27: Functional Analysis of its Binding Model towards its Applications as Detergent Additive |
title_sort |
alkaline protease from bacillus pumilus mp 27: functional analysis of its binding model towards its applications as detergent additive |
publisher |
Frontiers Media S.A. |
publishDate |
2016 |
url |
https://doi.org/10.3389/fmicb.2016.01195 https://doaj.org/article/43dabd77725c4095bffd669515512db5 |
long_lat |
ENVELOPE(-55.615,-55.615,49.517,49.517) |
geographic |
Southern Ocean Triton |
geographic_facet |
Southern Ocean Triton |
genre |
Southern Ocean |
genre_facet |
Southern Ocean |
op_source |
Frontiers in Microbiology, Vol 7 (2016) |
op_relation |
http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01195/full https://doaj.org/toc/1664-302X 1664-302X doi:10.3389/fmicb.2016.01195 https://doaj.org/article/43dabd77725c4095bffd669515512db5 |
op_doi |
https://doi.org/10.3389/fmicb.2016.01195 |
container_title |
Frontiers in Microbiology |
container_volume |
7 |
_version_ |
1766207180799737856 |