Cargando…
Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes
The current increase in the vast amount of marine crustacean shell waste produced by the fish processing industries has led to the need to find new methods for its disposal. Hence, the present study was carried out via marine shell wastes as substrate for protease production. The maximum production...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4980707/ https://www.ncbi.nlm.nih.gov/pubmed/28352581 http://dx.doi.org/10.1016/j.btre.2015.10.009 |
_version_ | 1782447501665632256 |
---|---|
author | Maruthiah, Thirumalai Somanath, Beena Immanuel, Grasian Palavesam, Arunachalam |
author_facet | Maruthiah, Thirumalai Somanath, Beena Immanuel, Grasian Palavesam, Arunachalam |
author_sort | Maruthiah, Thirumalai |
collection | PubMed |
description | The current increase in the vast amount of marine crustacean shell waste produced by the fish processing industries has led to the need to find new methods for its disposal. Hence, the present study was carried out via marine shell wastes as substrate for protease production. The maximum production (4000.65 U/ml) from Bacillus sp. APCMST-RS3 was noticed in 3:1% shrimp and oyster shell powder (SOSP) as substrate. Purified protease showed 53.22% and 22.66% enzyme yield; 3.48 and 8.49 fold purity with 40 kDa molecular weight; whereas, its K(m) and V(max) values were 0.6666 g/l, 1111.11 U/ml. This enzyme showed optimum activity at pH 9 and 60 °C temperature. Also, it retained maximum protease activity in the presence of NaCl (2.5 M), surfactants (Tween 20, 40, 60, 80 and SDS) and metal ions (MnCl(2), CaCl(2), HgCl(2) and BaCl(2)) and solvents. The candidate bacterium effectively deproteinized (84.35%) shrimp shell and its antioxidant potentials. |
format | Online Article Text |
id | pubmed-4980707 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-49807072017-03-28 Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes Maruthiah, Thirumalai Somanath, Beena Immanuel, Grasian Palavesam, Arunachalam Biotechnol Rep (Amst) Article The current increase in the vast amount of marine crustacean shell waste produced by the fish processing industries has led to the need to find new methods for its disposal. Hence, the present study was carried out via marine shell wastes as substrate for protease production. The maximum production (4000.65 U/ml) from Bacillus sp. APCMST-RS3 was noticed in 3:1% shrimp and oyster shell powder (SOSP) as substrate. Purified protease showed 53.22% and 22.66% enzyme yield; 3.48 and 8.49 fold purity with 40 kDa molecular weight; whereas, its K(m) and V(max) values were 0.6666 g/l, 1111.11 U/ml. This enzyme showed optimum activity at pH 9 and 60 °C temperature. Also, it retained maximum protease activity in the presence of NaCl (2.5 M), surfactants (Tween 20, 40, 60, 80 and SDS) and metal ions (MnCl(2), CaCl(2), HgCl(2) and BaCl(2)) and solvents. The candidate bacterium effectively deproteinized (84.35%) shrimp shell and its antioxidant potentials. Elsevier 2015-11-05 /pmc/articles/PMC4980707/ /pubmed/28352581 http://dx.doi.org/10.1016/j.btre.2015.10.009 Text en © 2015 Published by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Maruthiah, Thirumalai Somanath, Beena Immanuel, Grasian Palavesam, Arunachalam Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title | Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title_full | Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title_fullStr | Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title_full_unstemmed | Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title_short | Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes |
title_sort | deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine bacillus sp. apcmst-rs3 using marine shell wastes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4980707/ https://www.ncbi.nlm.nih.gov/pubmed/28352581 http://dx.doi.org/10.1016/j.btre.2015.10.009 |
work_keys_str_mv | AT maruthiahthirumalai deproteinizationpotentialandantioxidantpropertyofhaloalkalophilicorganicsolventtolerantproteasefrommarinebacillusspapcmstrs3usingmarineshellwastes AT somanathbeena deproteinizationpotentialandantioxidantpropertyofhaloalkalophilicorganicsolventtolerantproteasefrommarinebacillusspapcmstrs3usingmarineshellwastes AT immanuelgrasian deproteinizationpotentialandantioxidantpropertyofhaloalkalophilicorganicsolventtolerantproteasefrommarinebacillusspapcmstrs3usingmarineshellwastes AT palavesamarunachalam deproteinizationpotentialandantioxidantpropertyofhaloalkalophilicorganicsolventtolerantproteasefrommarinebacillusspapcmstrs3usingmarineshellwastes |