DNase Variants for Detergent Stability

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Solution Overview

Problem

Current detergent compositions containing DNases lack stability in the presence of standard detergent components, such as surfactants and bleaches, limiting their effectiveness in cleaning processes like laundry and dishwashing due to instability and incompatibility with detergent components.

Innovation Solution

Development of DNase variants with specific mutations, such as Q14F, Q14Y, N16A, and others, which exhibit improved stability and activity in detergent compositions, including enhanced storage stability and wash performance, by modifying the amino acid sequence to maintain or enhance enzymatic activity in the presence of detergent components.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If DNase is added to detergent compositions, then cleaning performance is improved through biofilm removal, but stability and compatibility with detergent components deteriorate

Engineering Contradiction:
Improvecleaning performanceVSAvoidstability in detergent composition
Core Design Contradiction:
ProductivityVSReliability

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of DNase through site-directed mutagenesis. Specific mutations (e.g., Q14F, Q14Y, N16A, L27W, P39Q, K52M, T65Y, S66A-S66L, S68M-S68R, Y77H, T79H, T79Y, S82D, S98N, G99N, S106P, A125R, S130D, P144W, P144A, G145*, C148D, G149D, W154F, W154T, W154V, K160R, L181K, L181N, L181P, Y182G, Y182H, Y182P, Y182*) are introduced to enhance stability while maintaining DNase activity. This allows the enzyme to withstand detergent components like surfactants and bleaches, resolving the contradiction between cleaning effectiveness and compositional stability.

Inventive Principle:
Principle #35Parameter changes

2Productivity

If DNase is used in laundry and dishwashing processes, then biofilm breakdown is enhanced, but storage stability and compatibility with standard detergent components worsen

Engineering Contradiction:
Improvebiofilm breakdown efficiencyVSAvoidstorage stability
Core Design Contradiction:
ProductivityVSStability of the object's composition

Solution Approach 1:

The invention modifies the biochemical parameters of DNase through amino acid substitution to achieve both improved storage stability and maintained biofilm degradation capability. The mutated variants demonstrate enhanced resistance to detergent conditions while retaining catalytic activity against eDNA in biofilms, effectively resolving the contradiction between storage stability and functional efficiency.

Inventive Principle:
Principle #35Parameter changes

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The DNase variants demonstrate increased stability and activity, with a half-life improvement factor of at least 1.05 in detergent compositions, effectively breaking down biofilm and improving cleaning performance in laundry and dishwashing applications.

Implementation Method 1

Extracellular DNA (eDNA) is known to be a key component of biofilms. It has been shown that eDNA together with protein provides structural integrity to bacterial biofilm, and that treatment with DNaseI results in change in biofilm structure leading to loss of biofilm material

Methodology Applied
Scientific EffectEnzyme catalysis: Enzyme

Implementation Method 2

DNase variants exhibiting improved properties... DNase enzymes which are suitable for use in detergents... effectively breaking down biofilm

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Data Source

PatentUS20240060061A1Dnase variants
Publication Date: 2024.02.22 NOVOZYMES AS
  • US20240060061A1 patent drawing

AI summary

The present invention relates to polypeptide variants having DNase activity, as well as detergent compositions comprising the variants, use of the variants for cleaning, and methods for obtaining the variants.