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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Maruthiah, Thirumalai Palavesam, Arunachalam |
| Description | Country affiliation: India Author Affiliation: Maruthiah T ( Centre for Marine Science and Technology, Manonmaniam Sundaranar University, Rajakkamangalam-629 502, Kanyakumari District, Tamilnadu, India.); Palavesam A ( Department of Animal Science, Manonmaniam Sundaranar University, Tirunelveli 627 012, Tamilnadu, India. Electronic address: plavesh06@gmail.com.) |
| Abstract | Halophilic organic solvent tolerant protease (HOSP) producing Paracoccus saliphilus APCMST-CS5 was isolated from the marine sediment samples and identified through 16S rRNA sequence analysis. P. saliphilus APCMST-CS5 registered maximum HOSP production of 1,321.70U/ml in the medium contained the most significant parameters such as shrimp shell powder (SSP), CaCl , NaCl, and sardinella powder (SP), obtained through Placket-Burman and Response Surface Methods. HOSP was further purified to 22.68 fold purity with 29.71 U/mg specific activity and its molecular weight was 39kDa. The HOSP was stable at 60°C, 9.0 pH, 3.0M NaCl concentration and it also showed maximum activity at other tested parameters. Interestingly the purified HOSP showed better antibiofilm ability against tested pathogens. Also, the HOSP effectively deproteinized (85.64%) shrimp shell chitin which in turn maximum and exhibited higher antioxidant activity. The commercial and experimental shrimp shell chitin showed similar peak pattern in FTIR and C CP/MAS NMR spectral analysis. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 97 |
| e-ISSN | 18790003 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2017-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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