The Clorox Company

Susan A Anderson

Richard J Wiersema

Maha Y El-Sayed

Sheldon N Lewis

Eugene A Mizusawa

Fred A Heitfeld

Chihae Yang

Ayrookaram J Poulose

Daniel R Leiske

The invention provides an improved procedure for the precise quantitation of organic oxidants in a solution with hydrogen peroxide in which the peroxide is removed by the addition of catalase to scavenge the same. Surprisingly, the catalase does not affect the organic oxidant, and the procedure can accurately quantitate even minute amounts of the organic oxidant. The inventive method is especially effective in quantitating peracid generated enzymatically, although it can be used for chemically generated organic oxidants.

Method for quantitating organic peracid using catalase

Lipase is immobilized on surfaces to facilitate oil removal from the surfaces and to alter wettability of the surfaces. The lipase is isolatable from a Pseudomonas organism such as,ATCC 53552 or from an organism expressing a coding region found in or cloned from the Pseudomonas. A particularly preferred lipase has a molecular weight of about 30 to 35 kd and is resolvable as a single band by SDS gel electrophoresis. Lipase sorbed on fabric forms a fabric-lipase complex for oil stain removal. The lipase may be sorbed on fabric before or after an oil stain, and the lipase is active to hydrolyze an oil stain on dry fabric or fabric in laundering solutions. The sorbed lipase has enhanced stability to denaturation by surfactants and to heat deactivation, is resistant to removal from fabric during laundering, retains substantial activity after drying fabric at an elevated temperature, and retains activity during fabric storage or wear. Redeposition of oil and oil hydrolysis by-products during laundering of fabric is retarded by the lipase. Oil hydrolysis by-products are removable during laundering of fabric at a basic pH or in the presence of a surfactant.

Immobilization of pseudomonas lipase on surfaces for oil removal

The inactivation in a laundry solution of a hydrolase enzyme by surfactant is prevented by the presence in the laundry solution of an amount of a non-charged enzyme activating means selected from oily hydrocarbons, hydrolyzable fatty acid ester substrates for the enzyme, e.g., triglycerides, essentially lipophilic organic compounds which are not substrates for the enzyme and which bear a polar substituent, and non-ionic surfactants which lower the oil to enzyme critical minimum molar ratio required to activate the enzyme.

Hydrolase surfactant systems and their use in laundering

An enzymatic perhydrolysis system, useful for bleaching, has a novel enzyme, a substrate, and a source of hydrogen peroxide, and provides in situ formation of peracid in aqueous solution. The substrate is selected for enzyme catalyzed reaction, and preferably is an acylglycerol with two or three fatty acid chains. The enzyme is hydrolytically and perhydrolytically active even in the presence of anionic surfactants, has lipase activity, and is modified from an enzyme isolatable from Pseudomonas putida ATCC 53552.

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Menlo Park, CA, United States of America

Susan A Anderson