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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.
Afiliación
  • Maruthiah T; Centre for Marine Science and Technology, Manonmaniam Sundaranar University, Rajakkamangalam, 629 502 Kanyakumari District, Tamil nadu, India.
  • Somanath B; Department of Zoology, Rani Anna Government College for Women, Manonmaniam Sundaranar University, Tirunelveli, 627 012 Tamil nadu, India.
  • Immanuel G; Centre for Marine Science and Technology, Manonmaniam Sundaranar University, Rajakkamangalam, 629 502 Kanyakumari District, Tamil nadu, India.
  • Palavesam A; Department of Animal Science, Manonmaniam Sundaranar University, Tirunelveli, 627 012 Tamil nadu, India.
Biotechnol Rep (Amst) ; 8: 124-132, 2015 Dec.
Article en En | MEDLINE | ID: mdl-28352581
ABSTRACT
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 31% 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 Km and Vmax 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 (MnCl2, CaCl2, HgCl2 and BaCl2) and solvents. The candidate bacterium effectively deproteinized (84.35%) shrimp shell and its antioxidant potentials.
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Texto completo: 1 Base de datos: MEDLINE Idioma: En Revista: Biotechnol Rep (Amst) Año: 2015 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Idioma: En Revista: Biotechnol Rep (Amst) Año: 2015 Tipo del documento: Article