AI Article Synopsis
- This study explored how different proteases (neutrase, papain, trypsin, and novozym 11028) and enzymolysis times affect the properties of hydrolysates from salmon milts.
- Findings revealed that longer enzymolysis times generally increase the fluorescence, solubility, and emulsifying properties of the hydrolysates, with trypsin producing the best results in protein recovery and degree of hydrolysis.
- The hydrolysates displayed varying structural and functional characteristics, indicating their potential use as functional food ingredients or nutraceuticals, with neutrase showing strong antioxidant potential and papain having the highest emulsifying stability.
Article Abstract
In this study, hydrolysates were obtained from salmon milts using four proteases (neutrase, papain, trypsin and novozym 11028). The effects of protease type and enzymolysis time (30, 60, 90, and 120 min) on the structural characteristics and functional properties of the hydrolysates were assessed. The fluorescence intensity of all hydrolysates increased as the extension of enzymolysis time, accompanied by an increase in solubility, emulsifying and foaming ability. Trypsin-hydrolysates showed the highest protein recovery and degree of hydrolysis (DH). The electrophoresis indicated that papain-hydrolysates contained more aggregates (>60 kDa), which was confirmed by larger particle size and lower DH. Neutrase-hydrolysate exhibited the smallest particle size and the highest emulsifying and foaming ability, while the highest emulsifying stability appeared in papain-hydrolysates. Neutrase-hydrolysate displayed the strongest antioxidant potential while papain-hydrolysate possessed the weakest. Results demonstrated that the salmon milt protein hydrolysates can be utilized as nutraceutical and functional food ingredients.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.foodchem.2024.141154 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Time-Resolved Levodopa Cascade Polymerization Tuned by Bimetallic MOF Fluorescent Nanozyme and Boric Acid for Butyrylcholinesterase Activity Dual-Mode Assay.
Anal Chem
December 2024
Department of Pharmacy, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan 430071, China.
A ratiometric fluorescence-photothermal dual-mode assay method is constructed for the detection of butyrylcholinesterase (BChE) activity based on time-resolved levodopa (L-DOPA) cascade polymerization. First, a newly designed bimetallic metal-organic framework (MOF), Eu/Co-DPA (DPA: pyridine-2,6-dicarboxylic acid), is screened out as a fluorescent nanozyme with high catalytic activity and superior luminescence properties. In the presence of boric acid (BA), L-DOPA forms BA-esterified L-DOPA, which is catalyzed by Eu/Co-DPA to form the oligomers with strong blue fluorescence.
View Article and Find Full Text PDFIdentification of Peptides from Edible Mushroom Feet and the Effect of Delaying D-Galactose-Induced Senescence of PC12 Cells Through TLR4/NF-κB/MAPK Signaling Pathways.
Foods
November 2024
Key Laboratory of Geriatric Nutrition and Health Ministry of Education, Beijing Technology and Business University, Beijing 100048, China.
mushroom has been proven to have anti-aging bioactivities. However, few studies have focused on edible mushroom feet peptides (PEMFPeps). In this paper, the effects of delaying the senescence of D-Galactose-induced PC12 cells were evaluated, and the mechanisms were also investigated.
View Article and Find Full Text PDFThe heterogeneous expression, extraction, and purification of recombinant Caldanaerobacter subterraneus subsp. tengcongensis apurine/apyrimidine endonuclease in Escherichia coli.
Protein Expr Purif
February 2025
Laboratory of Molecular Precision Diagnosis, Chengdu Base Cipher Biotechnology Co., Ltd., No. 618, Fenghuang Road, Shuangliu District, Chengdu, Sichuang, China. Electronic address:
Thermostable apurinic/apyrimidinic (AP) endonuclease (TtAP), cloned from Caldanaerobacter subterraneus subsp. tengcongensis, is an exonuclease III (Exo III) family protein with high-heat resistance, has activities of AP site endonuclease, 3'-5' exonuclease, and 3'-nuclease, and facilitates efficient amplification of lengthy DNA fragments in PCR. However, the research of the combinant TtAP in Escherichia coli with its expression, large-scale extraction and purification of its protein was limited.
View Article and Find Full Text PDFPreparation of enzymatic hydrolysates of mulberry leaf flavonoids and investigation into its treatment and mechanism for zebrafish inflammatory bowel disease.
Fish Shellfish Immunol
November 2024
Department of Pharmacognosy, School of Pharmacy, Hebei Medical University, 361 East Zhongshan Road, Shijiazhuang, Hebei, 050017, PR China. Electronic address:
Article Synopsis
- The study highlights the rising incidence of inflammatory bowel disease (IBD) and investigates the impact of flavonoids from mulberry leaves, particularly their enhanced anti-inflammatory effects after enzymatic hydrolysis.
- An enzymatic method was employed to create a hydrolysate of mulberry leaf flavonoids (EMLF), which showed superior protective effects against IBD in zebrafish compared to unhydrolyzed leaves, with mechanisms linked to purine metabolism regulation.
- The findings indicate that enzymatic deglycosylation effectively boosts the anti-inflammatory properties of mulberry leaves, suggesting potential strategies for utilizing natural products in IBD treatment.
Innovative insights into the enzymatic hydrolysis of salmon milt: Structural and functional analysis influenced by protease type and enzymolysis time.
Food Chem
January 2025
College of Animal Veterinary Medicine, Yunnan Agricultural University, Kunming, Yunnan 650201, China. Electronic address:
Article Synopsis
- This study explored how different proteases (neutrase, papain, trypsin, and novozym 11028) and enzymolysis times affect the properties of hydrolysates from salmon milts.
- Findings revealed that longer enzymolysis times generally increase the fluorescence, solubility, and emulsifying properties of the hydrolysates, with trypsin producing the best results in protein recovery and degree of hydrolysis.
- The hydrolysates displayed varying structural and functional characteristics, indicating their potential use as functional food ingredients or nutraceuticals, with neutrase showing strong antioxidant potential and papain having the highest emulsifying stability.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!