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Structure, physicochemical properties, and biological activities of protein hydrolysates from Zanthoxylum seed
Journal of the science of food and agriculture, 2024-04, Vol.104 (6), p.3329-3340
Dong, Si‐Yu
Li, Ying‐Qiu
Sun, Xin
Sun, Gui‐Jin
Wang, Chen‐Ying
Liang, Yan
Hua, Dong‐Liang
Chen, Lei
Mo, Hai‐Zhen
2024
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Dong, Si‐Yu
Li, Ying‐Qiu
Sun, Xin
Sun, Gui‐Jin
Wang, Chen‐Ying
Liang, Yan
Hua, Dong‐Liang
Chen, Lei
Mo, Hai‐Zhen
Titel
Structure, physicochemical properties, and biological activities of protein hydrolysates from Zanthoxylum seed
Ist Teil von
Journal of the science of food and agriculture, 2024-04, Vol.104 (6), p.3329-3340
Ort / Verlag
Chichester, UK: John Wiley & Sons, Ltd
Erscheinungsjahr
2024
Quelle
MEDLINE
Beschreibungen/Notizen
BACKGROUND Zanthoxylum seed, as a low‐cost and easily accessible plant protein resource, has good potential in the food industry. But protein and its hydrolysates from Zanthoxylum seed are underutilized due to the dearth of studies on them. This study aimed to investigate the structure and physicochemical and biological activities of Zanthoxylum seed protein (ZSP) hydrolysates prepared using Protamex®, Alcalase®, Neutrase®, trypsin, or pepsin. RESULTS Hydrolysis using each of the five enzymes diminished average particle size and molecular weight of ZSP but increased random coil content. ZSP hydrolysate prepared using pepsin had the highest degree of hydrolysis (24.07%) and the smallest molecular weight (<13 kDa) and average particle size (129.80 nm) with the highest solubility (98.9%). In contrast, ZSP hydrolysate prepared using Alcalase had the highest surface hydrophobicity and foaming capacity (88.89%), as well as the lowest foam stability (45.00%). Moreover, ZSP hydrolysate prepared using Alcalase exhibited the best hydroxyl‐radical scavenging (half maximal inhibitory concentration (IC50) 1.94 mg mL−1) and ferrous‐ion chelating (IC50 0.61 mg mL−1) activities. Additionally, ZSP hydrolysate prepared using pepsin displayed the highest angiotensin‐converting enzyme inhibition activity (IC50 0.54 mg mL−1). CONCLUSION These data showed that enzyme hydrolysis improved the physicochemical properties of ZSP, and enzymatic hydrolysates of ZSP exhibited significant biological activity. These results provided validation for application of ZSP enzymatic hydrolysates as antioxidants and antihypertensive agents in the food or medicinal industries. © 2023 Society of Chemical Industry.
Sprache
Englisch
Identifikatoren
ISSN: 0022-5142
eISSN: 1097-0010
DOI: 10.1002/jsfa.13218
Titel-ID: cdi_proquest_miscellaneous_2902945251
Format
–
Schlagworte
Angiotensin
,
Angiotensin-Converting Enzyme Inhibitors - chemistry
,
Antihypertensives
,
Antioxidants - chemistry
,
Antioxidants - pharmacology
,
biological activities
,
Biological activity
,
Biological effects
,
Biological properties
,
Chelation
,
enzymatic hydrolysates
,
Enzymes
,
Foaming
,
Food industry
,
Hydrolysates
,
Hydrolysis
,
Hydrophobicity
,
Molecular weight
,
Particle size
,
Pepsin
,
Pepsin A - metabolism
,
Physicochemical properties
,
Protein Hydrolysates - chemistry
,
Proteins
,
Random coil
,
Scavenging
,
Seeds - metabolism
,
structure characteristics
,
Subtilisin
,
Subtilisins - chemistry
,
Trypsin
,
Zanthoxylum
,
Zanthoxylum seed protein
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