Northern Shrimp Cathepsin L for Neutral pH Protein Modification
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Solution Overview
Problem
Current cathepsin L enzymes have limited activity under neutral to alkaline conditions and high temperatures, which restricts their application in modifying protein materials without causing denaturation, especially in food products, detergents, and medicaments.
Innovation Solution
A novel cathepsin L-like cysteine protease enzyme is extracted and purified from northern shrimp, exhibiting high activity at neutral to alkaline pH and low temperatures, allowing for effective collagen degradation and modification of protein materials without denaturation.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional cathepsin L enzymes are used, then they show potent endoprotease activity under acidic conditions, but they have limited activity under neutral to alkaline conditions and high temperatures
Solution Approach 1:
The patent applies parameter changes by modifying the enzyme's optimal operating conditions through the discovery of a novel cathepsin L-like enzyme from northern shrimp that operates optimally at neutral to alkaline pH (7-8) and low temperatures (35°C), contrasting with conventional cathepsin L enzymes that require acidic conditions (pH 2-4) and higher temperatures (50-70°C). This fundamental parameter shift enables the enzyme to function in diverse applications including food processing, detergents, and cosmetics where neutral to alkaline conditions are standard.
2Productivity
If high temperature is applied to enhance enzyme activity, then reaction speed increases, but protein denaturation occurs
Solution Approach 1:
The patent resolves this contradiction by changing the temperature parameter to optimal low temperature range (35°C or lower) for the northern shrimp cathepsin L-like enzyme. This temperature optimization maintains high enzymatic activity while preventing protein denaturation, as the enzyme's cold-adapted nature allows it to function efficiently at temperatures where conventional enzymes would be too slow but before denaturation occurs.
Solution Approach 2:
The patent employs a cold-adapted enzyme that operates effectively at low temperatures, eliminating the need for high-temperature processing that would require additional energy input and equipment. The enzyme achieves high productivity under mild conditions, making the process more energy-efficient and suitable for temperature-sensitive applications.
3Power
If acidic conditions are used for cathepsin L activity, then endoprotease activity is potent, but application to food products and cosmetics is restricted due to denaturation risks
Solution Approach 1:
The patent fundamentally changes the pH parameter from acidic (pH 2-4) to neutral to alkaline (pH 7-8) by utilizing the northern shrimp cathepsin L-like enzyme. This pH shift eliminates the harmful acidic conditions that cause protein denaturation while maintaining potent protease activity, enabling safe application in food products, cosmetics, and other pH-sensitive industries.
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 cathepsin L-like cysteine protease from northern shrimp demonstrates optimal activity at pH 7-8 and 35°C, maintaining stability and functionality, enabling its use in various applications such as food processing, cosmetics, and pharmaceuticals without protein denaturation.
Implementation Method 1
Protease is a generic term for enzymes that hydrolyze peptide bonds of proteins... cathepsin L-like cysteine protease enzyme... exhibiting high activity at neutral to alkaline pH and low temperatures, allowing for effective collagen degradation and modification of protein materials
Data Source
AI summary
The object of the present invention is to find and produce cathepsin L having high activity under neutral to alkaline conditions and at a low temperature range. The present inventors succeeded in discovering novel cathepsin L having activity even at a low temperature range from hepatopancreas of Japanese northern shrimp. The present inventors further determined the gene sequence encoding said novel cathepsin L, thus enabling production thereof by genetic recombination.