Thermostable Proline-Specific Endoprotease for Beer Haze Reduction
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Solution Overview
Problem
Current proline-specific endoproteases have limitations in thermostability and efficiency, particularly in applications like beer production and gluten degradation, where higher temperatures and effective haze reduction are required.
Innovation Solution
A thermostable proline-specific endoprotease derived from Rasamsonia emersonii, with enhanced residual activity at elevated temperatures, is developed, which can efficiently hydrolyze gluten and reduce haze-active proteins during the mashing process in beer production.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Temperature
If conventional proline-specific endoproteases are used, then they can perform basic proteolysis functions, but they exhibit poor thermostability and lose activity at elevated temperatures
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the proline-specific endoprotease to enhance its thermostability. Specifically, the enzyme from Rasamsonia emersonii contains amino acid substitutions that increase its stability at elevated temperatures compared to conventional enzymes, allowing it to maintain activity in the 50-70°C range typical of beer mashing processes.
2Productivity
If conventional proline-specific endoproteases are used, then they can degrade gluten and haze-active proteins, but they lack sufficient efficiency and activity at process-relevant temperatures
Solution Approach 1:
The patent improves productivity by changing the thermal stability parameter of the enzyme, which indirectly enhances its effective productivity at process temperatures. The thermostable enzyme maintains higher residual activity during the mashing process, leading to more efficient degradation of gluten and haze-active proteins compared to conventional enzymes that denature at these temperatures.
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 thermostable proline-specific endoprotease from Rasamsonia emersonii exhibits improved stability and activity at higher temperatures, effectively degrading haze-active proteins and gluten, enhancing the quality of beer by preventing haze formation and reducing gluten toxicity, thus addressing the limitations of existing enzymes.
Implementation Method 1
Proline-specific endoproteases are enzymes that hydrolyse a protein or peptide at a position where there is a proline in the protein or peptide
Data Source
AI summary
The present invention relates to a polypeptide having proline-specific endoprotease activity, selected from the group consisting ofi. a polypeptide comprising a mature polypeptide sequence of SEQ ID NO: 2;ii. a polypeptide that has least 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to the mature polypeptide sequence of SEQ ID NO: 2;iii. a polypeptide encoded by a nucleic acid that hybridizes under medium stringency, preferably under high stringency conditions to the complementary strand of the mature polypeptide coding sequence of SEQ ID NO:1;iv. a polypeptide encoded by a nucleic acid that has at least 70%, 75% 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the mature polypeptide coding sequence of SEQ ID NO: 1.The invention further relates to a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.