ArticleMolecules (Basel, Switzerland)2024
Optimization of Black Garlic Protein Extraction Process and Exploration of Its Properties and Functions with Enzymatic Hydrolysis Products.
Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The underexplored role of neuropilins in chronic pain pathophysiology: a review.Molecular biology reports · 2026Review
- Dietary Sheep Blood Zymolysate Modulates Gut Barrier Integrity, Microbiota Composition, and Nutritional Metabolism in Common Carp (Aquaculture nutrition · 2026Article
- A magnetic SERS aptasensor integrated with FeMikrochimica acta · 2025Article
- Preparation of an exogenous additive from Psoralea corylifolia fruit and its flavor-modifying effects on cigar tobacco leaves.Scientific reports · 2025Article
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9 authors.
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Abstract
This study optimized the process of extracting protein from black garlic using an alkaline dissolution and acid precipitation method through response surface methodology. The optimal extraction conditions were determined as a solid-to-liquid ratio of 1:50, an extraction time of 100 min, an extraction temperature of 30 °C, and an alkaline extraction pH of 9.0. Under these optimized conditions, the actual black garlic protein (BGP) extraction yield was 12.10% ± 0.21%, and the isoelectric point of the obtained BGP was 3.1. Subsequently, this study extracted black garlic protein under optimal conditions and subjected it to enzymatic hydrolysis using different enzymes (trypsin, pepsin, and their mixed enzymes). The functional characteristics, antioxidant activity, and hypoglycemic activity of black garlic protein before and after enzymatic hydrolysis were compared. Among the hydrolysates, the pepsin hydrolysate (BGPH-P) had the smallest particle size (188.57 ± 1.93 nm) and the highest Zeta potential (-29.93 ± 0.42 mV). Scanning electron microscopy showed that BGPH-P had the smallest and most dispersed particles. Fourier-transform infrared (FTIR) spectroscopy revealed that the dual enzymatic hydrolysis hydrolysate (BGPH-PT) exhibited the most stable structure. Compared to BGP, the hydrolysates demonstrated significantly improved solubility, water-holding capacity, and foaming ability (
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