Tryptophan-Enriched Lysozyme Hydrolysate for High Trp/LNAA Ratios
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Solution Overview
Problem
Current methods for increasing brain serotonin levels through tryptophan supplementation are limited by the need for high Trp/LNAA ratios, which are difficult to achieve with existing protein preparations like alpha-lactalbumin due to contamination issues and high costs, and are further restricted by regulatory constraints on free tryptophan use.
Innovation Solution
A composition comprising a combination of peptide-bound and polypeptide-bound tryptophan fractions derived from hen egg lysozyme, with a high Trp/LNAA ratio, which includes a water-soluble peptide fraction and a protease-resistant polypeptide fraction, allowing for rapid and sustained increases in plasma Trp/LNAA ratios.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Quantity of substance
If free tryptophan is used to increase plasma tryptophan levels, then the Trp/LNAA ratio can be improved, but regulatory constraints limit the allowable levels in various application forms
Solution Approach 1:
The patent uses peptidically bound tryptophan in the form of small peptides (particularly dipeptides and tripeptides) as a temporary, easily degradable alternative to free tryptophan. These small peptides are rapidly hydrolyzed in the gastrointestinal tract to release free tryptophan, providing a compliant way to increase plasma tryptophan levels without directly adding regulated free tryptophan.
Solution Approach 2:
The patent pre-hydrolyzes lysozyme to generate small tryptophan-containing peptides before administration. This preliminary enzymatic hydrolysis creates a preparation that will rapidly release tryptophan in the body, achieving the desired plasma tryptophan elevation effect while avoiding regulatory issues with direct free tryptophan supplementation.
2Quantity of substance
If alpha-lactalbumin preparations are used to increase tryptophan concentration, then plasma tryptophan levels improve, but the Trp/LNAA ratio is not sufficiently optimized due to contamination with beta-lactoglobulin
Solution Approach 1:
The patent extracts and utilizes only the tryptophan-containing peptide fraction from lysozyme hydrolysis, separating it from the rest of the protein structure. This extraction approach allows obtaining a preparation enriched in tryptophan while eliminating the contamination issue inherent in alpha-lactalbumin preparations that contain beta-lactoglobulin.
Solution Approach 2:
The patent changes the degree of hydrolysis parameter to produce small peptides (low molecular weight) from lysozyme. By controlling hydrolysis to achieve DH values that generate predominantly di- and tripeptides, the preparation achieves high tryptophan availability and optimal Trp/LNAA ratio, distinguishing it from alpha-lactalbumin preparations.
3Productivity
If extensive hydrolysis of lysozyme is performed to generate small peptides, then absorption and utilization of tryptophan is improved, but the preparation may lose protease resistance and structural integrity
Solution Approach 1:
The patent optimizes the degree of hydrolysis (DH) parameter to achieve a balance between peptide size and functional properties. By controlling hydrolysis to produce small peptides (dipeptides and tripeptides) rather than complete hydrolysis to free amino acids, the preparation maintains some structural organization while achieving rapid absorption, and the protease resistance is actually improved due to the small peptide size being less susceptible to further degradation.
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 composition effectively generates high and prolonged Trp/LNAA ratios in the blood, providing clinical benefits for mood, cognition, alertness, and sleep quality, while being cost-effective and compliant with regulatory standards.
Implementation Method 1
A composition comprising a combination of peptide-bound and polypeptide-bound tryptophan fractions derived from hen egg lysozyme, with a high Trp/LNAA ratio, which includes a water-soluble peptide fraction and a protease-resistant polypeptide fraction, allowing for rapid and sustained increases in plasma Trp/LNAA ratios.
Data Source
AI summary
The present disclosure relates to a composition, and method thereof, which comprises tryptophan whereby 10 to 90%, preferably 20 to 80% of the tryptophan is present as free tryptophan or peptide-bound tryptophan and 10 to 90%, preferably 20 to 80% of the tryptophan is present as polypeptide-bound tryptophan.