Camel Chymosin Stability via Protein Stabilizers
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Solution Overview
Problem
Existing milk clotting aspartic protease enzyme compositions face challenges in maintaining physical stability and specific activity, particularly during storage and transportation, where enzymes are subjected to physical forces that can lead to denaturation and loss of activity.
Innovation Solution
The addition of specific polypeptide or protein formulations, such as whey protein or ovalbumin, to aspartic protease enzymes like chymosin significantly enhances both the physical stability and specific activity of the enzyme compositions, with optimal effects observed at concentrations above 0.01% (w/w) and for polypeptides longer than 10 amino acids.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If milk clotting aspartic protease enzyme compositions are stored and transported, then the enzymes are exposed to physical forces, but this leads to denaturation and loss of activity
Solution Approach 1:
The patent introduces stabilizing agents (polypeptides/proteins) as intermediary substances that mediate between the enzyme and physical stress. These stabilizers form protective complexes with the aspartic protease, shielding it from denaturation during storage and transportation, thereby resolving the contradiction between maintaining enzyme activity and withstanding physical forces
Solution Approach 2:
The patent applies beforehand cushioning by pre-formulating the enzyme composition with stabilizing agents before exposure to physical stress. The stabilizers are incorporated into the composition in advance, creating a protective environment that cushions the enzyme against upcoming physical forces during storage and transport
2Reliability
If polypeptide/protein formulations are added to aspartic protease enzymes, then physical stability and specific activity increase, but the composition complexity increases
Solution Approach 1:
The patent applies parameter changes by optimizing the concentration ranges of polypeptides/proteins (0.01-10% w/w) and selecting specific molecular weight ranges (>10 amino acids). By defining precise parameter boundaries, the patent achieves enhanced physical stability while controlling composition complexity through quantifiable specifications rather than open-ended formulation
3Reliability
If polypeptide/protein formulations are added to aspartic protease enzymes, then specific activity increases, but the amount of substance in the composition increases
Solution Approach 1:
The patent optimizes the concentration parameter of polypeptides/proteins to achieve maximum specific activity enhancement with minimal substance addition. The specified range of 0.01-10% w/w represents an optimized parameter window where sufficient stabilizer is present to boost specific activity while keeping the total substance quantity economically viable
Solution Approach 2:
The patent creates a composite enzyme formulation where polypeptides/proteins work synergistically with aspartic protease. This composite approach allows the stabilizers to enhance specific activity through molecular interactions rather than simply adding bulk, achieving activity enhancement efficiency that outweighs the substance quantity increase
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 inclusion of these polypeptides increases the conformational stability of the enzymes, resulting in higher retained activity and specific activity, even under conditions of physical stress like shaking, and demonstrates improved stability and activity for both camel and bovine chymosins, suggesting a general applicability to similar milk clotting aspartic protease enzymes.
Implementation Method 1
The inclusion of these polypeptides increases the conformational stability of the enzymes, resulting in higher retained activity and specific activity
Implementation Method 2
the aspartic protease has increased physical stability... by adding suitable polypeptide/protein formulations... one significantly improves the physical stability and possibly the specific activity of the enzyme compositions
Data Source
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AI summary
A liquid or dried granulated milk clotting aspartic protease enzyme composition comprising added polypeptides/proteins. The polypeptides/proteins may be animal-derived (e.g. whey, lactalbumin, transferrin, casein, ovalbumin, gelatin, blood), vegetable-derived (soy, pea, corn, potato, hemp, rice, wheat, peanut, sun flower, rape seed) or algae proteins (e.g. spirulina). Addition of protein in several instances increases activity of the enzyme and simultaneously improves physical stability.