Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8922
Title: Evaluation of a New Lipase from Staphylococcus sp. for Detergent Additive Capability
Authors: Chauhan, Mamta
Chauhan, Rajinder Singh
Garlapati, Vijay Kumar
Keywords: Lipase
Staphylococcus sp.
Detergent Additive
Issue Date: 2013
Publisher: Jaypee University of Information Technology, Solan, H.P.
Abstract: Lipases are the enzymes of choice for laundry detergent industries owing to their triglyceride removing ability from the soiled fabric which eventually reduces the usage of phosphate-based chemical cleansers in the detergent formulation. In the present study, a partially purified bacterial lipase from Staphylococcus arlettae JPBW-1 isolated from the rock salt mine has been assessed for its triglyceride removing ability by developing a presoak solution so as to use lipase as an additive in laundry detergent formulations. The effects of selected surfactants, commercial detergents, and oxidizing agents on lipase stability were studied in a preliminary evaluation for its further usage in the industrial environment. Partially purified lipase has shown good stability in presence of surfactants, commercial detergents, and oxidizing agents.Washing efficiency has been found to be enhanced while using lipase with 0.5% nonionic detergent than the anioinic detergent. The wash performance using 0.5% wheel with 40U lipase at 40∘C in 45 min results in maximum oil removal (62%) from the soiled cotton fabric. Hence, the present study opens the new era in enzyme-based detergent sector for formulation of chemical-free detergent using alkaline bacterial lipase.
URI: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8922
Appears in Collections:Journal Articles

Files in This Item:
File Description SizeFormat 
Evaluation of a new lipase from staphylococcus sp. for detergent additive capability.pdf1.27 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.