Cargando…

Isolation and immobilization of alkaline protease on mesoporous silica and mesoporous ZSM-5 zeolite materials for improved catalytic properties

Alkaline protease from brinjal leaf (Solanum melongena) having milk clotting activity has been purified to 9.44 fold to a final specific activity of 45.71 U/mg. SDS-PAGE of the final preparation revealed a single protein band of approx 14 kDa. Purified enzyme was characterized and was successfully i...

Descripción completa

Detalles Bibliográficos
Autores principales: Kumari, Arpana, Kaur, Balwinder, Srivastava, Rajendra, Sangwan, Rajender S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5668643/
https://www.ncbi.nlm.nih.gov/pubmed/29124151
http://dx.doi.org/10.1016/j.bbrep.2015.05.009
Descripción
Sumario:Alkaline protease from brinjal leaf (Solanum melongena) having milk clotting activity has been purified to 9.44 fold to a final specific activity of 45.71 U/mg. SDS-PAGE of the final preparation revealed a single protein band of approx 14 kDa. Purified enzyme was characterized and was successfully immobilized into the amorphous mesoporous silica (SBA-15) and crystalline mesoporous zeolite (Nano-ZSM-5) using entrapment method. Maximum immobilization of 63.5% and 79.77% was obtained with SBA-15 and Nano-ZSM-5, respectively. This protocol serves as a novel approach for bioprocesses, mainly as milk coagulant for local dairy products and particularly, cheese making, and opens the new dimension of further research and other innovation.