Wheat Gluten Hydrolysis and Quaternization Data for Hair Recovery

Experimental data details the enzymatic hydrolysis and cationization of wheat gluten to improve its binding with hair keratin. The study reports specific metrics, including a hydrolysate containing 58.71% short-chain peptides (<1000 Da) and a shift in isoelectric point from 7.0 to 10.0. The dataset, authored by Shukun Wang and published in 2020, supports research on protein modification for cosmetic applications.

Use Cases

• Analyze the relationship between the degree of hydrolysis and functional indices like foaming capacity or emulsion stability.
• Model the effect of cationization on the isoelectric point shift from 7.0 to 10.0 for protein adhesion studies.
• Investigate the correlation between the 58.71% short-chain peptide content and performance metrics in hair recovery tests.
• Study the impact of enzymatic conditions (pH 8.2, 55°C) on resulting nitrogen solubility and emulsifying activity indices.

Strengths

• Reports precise quantitative results, including a hydrolysate with 58.71% short-chain peptides (<1000 Da).
• Provides specific experimental conditions and measured indices, such as a foam stability index of 56.67% and an isoelectric point shift from 7.0 to 10.0.
• Dataset is published under a permissive CC0 1.0 license, allowing for unrestricted reuse.

Limitations

• The dataset scope is limited to a specific experimental study on wheat gluten modification, lacking broader protein or cosmetic ingredient comparisons.
• No raw tabular data or column descriptions are provided, limiting direct computational analysis.
• Data is from a single study published in 2020 and may not reflect the latest research in protein engineering.

Provenance

Source

Dryad digital repository.

Collection Method

Experimental laboratory data from a study on enzymatic hydrolysis and chemical cationization of wheat gluten.

Freshness

Last updated 2020-06-24.