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

dc.contributor.author	Kumari, A.
dc.contributor.author	Kaur, B.
dc.contributor.author	Srivastava, R.
dc.contributor.author	Sangwan, R.S.
dc.date.accessioned	2016-08-02T05:48:25Z
dc.date.available	2016-08-02T05:48:25Z
dc.date.issued	2016-08-02
dc.identifier.uri	http://localhost:8080/xmlui/handle/123456789/141
dc.description.abstract	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.	en_US
dc.language.iso	en_US	en_US
dc.subject	Alkaline protease	en_US
dc.subject	SBA-15	en_US
dc.subject	Nano-ZSM-5	en_US
dc.subject	Zeolite	en_US
dc.subject	Immobilization	en_US
dc.title	Isolation and immobilization of alkaline protease on mesoporous silica and mesoporous ZSM-5 zeolite materials for improved catalytic properties	en_US
dc.type	Article	en_US