Variant Phytase Enzymes for Feed Processing Stability

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Solution Overview

Problem

Phytase enzymes in animal feeds are not stable under high temperatures and acidic conditions, leading to inefficient phytate degradation and increased costs due to the need for external phosphorus supplementation, which also contributes to environmental pollution.

Innovation Solution

Development of variant phytases with specific amino acid substitutions that enhance thermostability and pH stability, allowing for improved activity and stability during feed processing and digestion, such as substitutions at positions 55, 157, 159, 255, 354, and 380, which result in enzymes that maintain activity at elevated temperatures and acidic pH levels.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional phytase is used in animal feeds, then phosphorus can be released from phytate, but the enzyme is inactivated by high temperatures during feed processing and by acidic conditions in the gastrointestinal tract

Engineering Contradiction:

Improveenzyme stabilityVSAvoidthermostability

Core Design Contradiction:

ReliabilityVSTemperature

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of phytase through site-directed mutagenesis. Specific amino acid residues are substituted to alter the enzyme's physical-chemical properties, particularly its thermal stability and pH resistance, enabling it to withstand feed processing temperatures and gastrointestinal acidic conditions while maintaining catalytic activity.

Inventive Principle:

Principle #35Parameter changes

Solution Approach 2:

The patent applies local quality by making targeted amino acid substitutions at specific positions in the phytase molecule rather than modifying the entire enzyme. This allows localized modification of stability properties while preserving the overall catalytic function, creating variants with improved thermostability and acid resistance at specific structural locations.

Inventive Principle:

Principle #3Local quality

2Reliability

If conventional phytase is used in animal feeds, then phosphorus can be released from phytate, but the enzyme is degraded by pepsin and other gastric proteases in the upper gastrointestinal tract

Engineering Contradiction:

Improveenzyme stabilityVSAvoidprotease degradation

Core Design Contradiction:

ReliabilityVSObject-affected harmful factors

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of phytase through site-directed mutagenesis. Specific amino acid residues are substituted to alter the enzyme's physical-chemical properties, particularly its resistance to proteolytic degradation while maintaining catalytic activity under gastrointestinal conditions.

Inventive Principle:

Principle #35Parameter changes

3Quantity of substance

If inorganic phosphorus is added to feeds for monogastric animals, then phosphorus deficiency can be prevented, but the cost of feed production increases significantly

Engineering Contradiction:

Improvephosphorus availabilityVSAvoidfeed production cost

Core Design Contradiction:

Quantity of substanceVSEase of manufacture

Solution Approach 1:

The patent applies self-service by enabling the phytase enzyme to automatically release bound phosphorus from phytate within the animal's gastrointestinal tract. This self-catalyzed phosphorus liberation eliminates the need for external inorganic phosphorus supplementation, reducing feed costs while maintaining phosphorus availability for monogastric animals.

Inventive Principle:

Principle #25Self-service

4Productivity

If conventional phytase is used in animal feeds, then phosphorus can be released from phytate, but the enzyme loses activity during feed pelleting due to high temperature and pressure

Engineering Contradiction:

Improvephytate degradation efficiencyVSAvoidenzyme activity retention

Core Design Contradiction:

ProductivityVSDuration of action of stationary object

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of phytase through site-directed mutagenesis. Specific amino acid residues are substituted to alter the enzyme's physical-chemical properties, particularly its thermal stability and pressure resistance, enabling it to withstand feed processing conditions while maintaining catalytic activity for phytate degradation.

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 variant phytases exhibit increased thermostability and pH stability, leading to improved phytate degradation and reduced phosphorus excretion in animal manure, thus enhancing nutritional value and reducing environmental impact while lowering production costs.

Implementation Method 1

Phytase is a phosphatase that catalyzes the hydrolysis of O—P bonds in phytate and releases inorganic usable phosphorous.

Methodology Applied

Scientific EffectHydrolysis: Hydrolysis

Implementation Method 2

Phytase is a phosphatase that catalyzes the hydrolysis of O—P bonds in phytate

Methodology Applied

Scientific EffectEnzyme catalysis: Enzyme

Data Source

PatentUS10351832B2Phytases and uses thereof

Publication Date: 2019.07.16 FORNIA BIOSOLUTIONS INC

AI summary

The present invention relates to variant phytase enzymes and their use thereof.