Lipolytic Enzyme Variant Stability in Detergent

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Solution Overview

Problem

Existing lipolytic enzymes used in detergents lack sufficient in-detergent stability, which affects their performance in maintaining enzyme activity in the presence of cleaning agents.

Innovation Solution

Development of lipolytic enzyme variants with specific amino acid substitutions at positions 27, 227, 231, and 233, enhancing their stability in detergent solutions, achieved through genetic modification and expression in host cells.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If lipolytic enzymes are used in detergents, then they can remove lipid or fatty stains from clothes, but they lack sufficient in-detergent stability and lose activity over time

Engineering Contradiction:
Improvein-detergent stabilityVSAvoidenzyme activity retention
Core Design Contradiction:
ReliabilityVSDuration of action of stationary object

Solution Approach 1:

The patent applies parameter changes by modifying specific amino acid residues at positions 27, 227, 231, and 233 of the lipase sequence to enhance in-detergent stability. These targeted substitutions change the local chemical environment and structural properties of the enzyme, allowing it to maintain activity longer in detergent formulations without requiring additional stabilizing agents or formulation changes.

Inventive Principle:
Principle #35Parameter changes

2Reliability

If amino acid substitutions are made to improve in-detergent stability, then enzyme activity is retained better, but the enzyme structure is modified which may affect other properties

Engineering Contradiction:
Improvein-detergent stabilityVSAvoidenzyme functionality
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The patent applies local quality by making targeted amino acid substitutions at specific positions (27, 227, 231, and 233) rather than global modifications. This localized approach allows the enzyme to gain improved detergent stability while preserving the overall catalytic structure and function. The substitutions are confined to specific regions that do not interfere with the active site or essential structural elements, thus maintaining versatility.

Inventive Principle:
Principle #3Local quality

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 variants demonstrate improved retention of lipase activity in detergent environments, maintaining functionality over time, even under storage conditions, compared to parent enzymes.

Implementation Method 1

cultivating the transformed host cell comprising the nucleic acid construct or the recombinant expression vector comprising the polypeptide under conditions conductive for the production of the variant

Methodology Applied
Scientific EffectGenetic expression:

Implementation Method 2

use of the lipolytic enzyme variant in the hydrolysis of a carboxylic acid ester or in the hydrolysis, synthesis or interesterification of an ester

Methodology Applied
Scientific EffectEnzymatic hydrolysis: Hydrolysis

Data Source

PatentEP2250258B1Lipolytic enzyme variant with improved stability and polynucleotides encoding same
Publication Date: 2017.01.04 NOVOZYMES AS
  • EP2250258B1 patent drawingFigure 1
  • EP2250258B1 patent drawingFigure 1
  • EP2250258B1 patent drawingFigure 1

AI summary

The invention provides lipolytic enzyme variants having improved in-detergent stability and polynucleotides encoding same. Lipolytic enzyme variants with improved in-detergent stability are obtained by substituting certain specified amino acid residues in a parent lipolytic enzyme.