Aminopeptidase Specificity for Targeted Protein Taste Modification
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
There is a growing need to modify the taste of protein-containing food products, and existing aminopeptidases do not exhibit the required substrate specificities to meet these demands.
Innovation Solution
Development of a novel aminopeptidase with specificities different from existing enzymes, derived from Aspergillus nidulans or Aspergillus oryzae, exhibiting optimal activity at around 50°C and pH 7-8, with high specificity for L-alanine or L-lysine residues.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Adaptability or versatility
If existing aminopeptidases are used for taste modification, then general protein decomposition occurs, but the substrate specificity required for diverse taste modification needs is not met
Solution Approach 1:
The invention segments the broad category of aminopeptidases into distinct types based on substrate specificity. By isolating and characterizing individual aminopeptidase variants with specific substrate preferences (e.g., leucine-specific, phenylalanine-specific), the patent creates specialized enzyme tools that can be selectively applied for precise taste modification without requiring a large inventory of different enzymes.
Solution Approach 2:
The patent applies local quality by endowing specific aminopeptidase variants with specialized substrate recognition capabilities. Each aminopeptidase is optimized to recognize and cleave specific amino acid sequences at protein N-termini, allowing targeted release of particular taste-active amino acids (umami, bitter, sweet) from protein substrates, thereby achieving diverse taste modification effects through localized enzymatic action.
2Manufacturing precision
If broad-spectrum aminopeptidases are used, then multiple amino acids are released, but control over specific taste components is reduced
Solution Approach 1:
The invention changes the specificity parameter of aminopeptidases by isolating variants with different substrate recognition profiles. By selecting aminopeptidases with specific kinetic parameters (Km, kcat) for particular amino acid substrates, the patent enables precise control over which taste components are released during protein decomposition, while maintaining high catalytic efficiency for the targeted substrates.
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 novel aminopeptidase effectively modifies the taste of food products by releasing alanine or lysine from proteins, offering unique taste modification capabilities not achievable with prior enzymes.
Implementation Method 1
Aminopeptidase is an enzyme (exopeptidase) that catalyzes the cleavage of amino acid units from the amino terminus (N-terminus) of proteins and peptides
Implementation Method 2
Aminopeptidase is an enzyme (exopeptidase) that catalyzes the cleavage of amino acid units from the amino terminus (N-terminus) of proteins and peptides
Data Source
Figure 1
Figure 2
Figure 3
AI summary
It is an object of the present invention to provide an enzyme agent containing a novel aminopeptidase exhibiting substrate specificity that is different from those of existing aminopeptidases. The present invention relates to an enzyme agent containing, as an active ingredient, an aminopeptidase consisting of the amino acid sequence as set forth in SEQ ID No: 1 or SEQ ID No: 8 or an amino acid sequence equivalent thereto. Moreover, the present invention relates to an enzyme agent containing, as an active ingredient, an aminopeptidase, which is derived from Aspergillus nidulans or Aspergillus oryzae and has the following physicochemical properties: (1) optimal temperature: around 50°C; (2) optimal pH: around pH 7 to 8; and (3) substrate specificity: having the highest specificity to L-alanine residue or L-lysine residue.