Phospholipase C Mutation for Higher Vegetable Oil Degumming Activity

Resolve Bottlenecks,
Find Innovative Solutions
Generate Solutions

Solution Overview

Problem

Existing phospholipase C enzymes used in vegetable oil degumming processes have limitations in enzyme activity and efficiency, leading to suboptimal oil yield and increased production costs.

Innovation Solution

Mutating the glycine at amino acid position 10 of BC-PC-PLC to aspartic acid, along with other specific mutations, results in a phospholipase C variant with significantly enhanced specific enzyme activity, improving degumming efficiency and DAG yield.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If phospholipase C enzyme is used in vegetable oil degumming process, then phospholipids can be hydrolyzed to improve oil quality, but the enzyme activity and degumming efficiency are insufficient leading to suboptimal oil yield

Engineering Contradiction:
Improvedegumming efficiencyVSAvoidenzyme activity
Core Design Contradiction:
ProductivityVSReliability

Solution Approach 1:

The patent applies parameter changes by mutating specific amino acid residues (Glycine to Aspartic acid at position 10, and other positions) in the phospholipase C enzyme sequence. This chemical parameter change at the molecular level fundamentally alters the enzyme's catalytic properties, increasing specific enzyme activity by 16-fold and improving overall degumming efficiency while maintaining enzyme stability and reliability.

Inventive Principle:
Principle #35Parameter changes

2Ease of manufacture

If conventional phospholipase C is used, then degumming process can be performed, but production costs increase due to suboptimal efficiency requiring more enzyme or repeated processing

Engineering Contradiction:
Improveproduction costVSAvoidoil yield
Core Design Contradiction:
Ease of manufactureVSProductivity

Solution Approach 1:

By changing the amino acid parameters of the enzyme through directed evolution and site-directed mutagenesis, the patent creates a hyper-active phospholipase C variant. This parameter change results in dramatically improved catalytic efficiency, allowing the degumming process to achieve higher oil yields while reducing the amount of enzyme required and minimizing production costs.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent replaces the conventional mechanical/chemical refining methods with an optimized enzymatic system. The mutated phospholipase C provides superior catalytic performance compared to traditional chemical degumming agents, achieving better oil yield and quality while reducing the need for additional processing steps and chemical additives, thereby lowering overall production costs.

Inventive Principle:
Principle #28Mechanics substitution (Replace mechanical system)

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 mutated phospholipase C variant achieves an 83% increase in specific enzyme activity without reducing degumming ability per unit enzyme activity, thereby enhancing oil yield and reducing production costs.

Implementation Method 1

PLC can specifically hydrolyze the phosphoglyceride bond at Sn-3 of a phospholipid and generate the corresponding diacylglycerol (DAG) and phosphatidic acids

Methodology Applied
Scientific EffectHydrolysis: Hydrolysis

Implementation Method 2

Phospholipase is an enzyme widely present in animals, plants, and microorganisms that can specifically hydrolyze glycerophospholipids

Methodology Applied
Scientific EffectEnzyme catalysis: Enzyme

Data Source

PatentEP3725878B1Phospholipase c and encoding gene thereof
Publication Date: 2026.04.01 WILMAR SHANGHAI BIOTECH RES & DEV CENT
  • EP3725878B1 patent drawingFigure 1~2
  • EP3725878B1 patent drawingFigure 3

AI summary

According to the present disclosure, on the basis of all existing mutations, the tenth glycine of a BC-PC-PLC is mutated into aspartic acid, a specific enzyme activity thereof is 83% higher than that of a sequence before the mutation, and protein expression and degumming activity of unit enzyme activity do not change, so as to further reduce manufacturing costs.