Modified Rapeseed Protein Through PAD-Mediated Deimination
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Solution Overview
Problem
Rapeseed protein is limited in food applications due to poor digestibility, taste, and nutritional value, primarily attributed to anti-nutritional factors like trypsin inhibitors and undesirable sensory characteristics such as bitterness and mouthfeel.
Innovation Solution
Treatment of rapeseed protein with protein arginine deiminase (PAD) to convert arginine residues into citrulline, reducing the activity of trypsin inhibitors and modifying sensory aspects like sweetness, astringency, and mouthfeel.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If rapeseed protein is used in food products, then vegetable-based protein alternative is provided, but poor digestibility and anti-nutritional factors reduce nutritional value
Solution Approach 1:
The patent applies peptidyl arginine deiminase (PAD) to convert arginine residues in trypsin inhibitors into citrulline residues, thereby deactivating the anti-nutritional factors. This transforms the harmful trypsin inhibitors into benign proteins that no longer inhibit digestion, effectively converting harm into benefit while preserving the protein structure
Solution Approach 2:
The patent changes the chemical parameter of specific amino acid residues (arginine to citrulline conversion) in the trypsin inhibitor proteins through enzymatic treatment. This parameter change at the molecular level alters the functional properties of the inhibitors, reducing their anti-nutritional activity while maintaining protein integrity
2Reliability
If rapeseed protein is used in food products, then vegetable-based protein alternative is provided, but undesirable sensory characteristics like bitterness and mouthfeel reduce taste quality
Solution Approach 1:
The patent utilizes PAD enzyme treatment to convert arginine residues in bitter-tasting proteins into citrulline, thereby transforming the harmful sensory characteristics (bitterness and undesirable mouthfeel) into beneficial properties. The citrullinated proteins exhibit improved taste profiles while the enzyme treatment process itself becomes a value-adding step
Solution Approach 2:
The patent changes the chemical composition parameter by modifying arginine residues to citrulline through enzymatic deimination. This parameter change at the amino acid level directly affects the sensory properties of the protein, reducing bitterness and improving mouthfeel characteristics
3Stability of the object's composition
If trypsin inhibitors are present in rapeseed protein, then protein structure is maintained, but protein digestibility is significantly reduced
Solution Approach 1:
The patent applies PAD treatment to convert arginine residues in trypsin inhibitors to citrulline, which deactivates the inhibitory function while preserving the overall protein structure. This allows the protein to maintain structural integrity for functional applications while eliminating the harmful digestive inhibition
Solution Approach 2:
The patent applies localized modification only to specific arginine residues involved in trypsin inhibition, rather than altering the entire protein structure. The PAD enzyme specifically targets the reactive site arginine residues, leaving the rest of the protein structure intact and functional
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
PAD-treated rapeseed protein exhibits significant reductions in sensory defects by 10% to 60% compared to untreated protein, improving digestibility and taste, making it suitable for food products.
Implementation Method 1
Treatment of rapeseed protein with protein arginine deiminase (PAD) to convert arginine residues into citrulline
Data Source
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AI summary
The present invention is directed to a modified rapeseed protein isolate and to a process for making a modified rapeseed protein isolate with the aid of a peptidyl arginine deiminase.