High-pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions
文献类型： 外文期刊
作者：
Gong, Kuijie
1
;
Deng, Lei
1
;
Shi, Aimin
1
;
Liu, Hongzhi
1
;
Liu, Li
1
;
Hu, Hui
1
;
Adhikari, Benu
3
;
Wang, Qiang
1
;
作者机构： 1.Chinese Acad Agr Sci, Inst Agroprod Proc & Technol, Key Lab Agroprod Proc, Minist Agr, POB 5109, Beijing 100193, Peoples R China
2.Shandong Acad Agr Sci, Crop Res Inst, Jinan 250100, Peoples R China
3.RMIT Univ, Sch Appl Sci, City Campus, Melbour
关键词： Angiotension converting enzyme inhibitory (ACEI);antihypertensive peptide;disaggregation;high-pressure microfludisation;peanut protein isolate
期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：3.713； 五年影响因子：3.408 ）
ISSN：
年卷期：
页码：
收录情况： SCI
摘要： High-pressure microfluidisation (HPM) pretreatment was applied to increase invitro antihypertensive activity of peanut peptide fractions (PPF). The morphology of protein in aqueous dispersion revealed that peanut protein isolate (PPI) disaggregated at relatively low pressure (<= 120 MPa) and re-aggregated at relatively high pressures (150-210 MPa). The treated pressure of 120 MPa could lead to the most disaggregation of PPI. Small peptides contents, trichloroacetic acid-nitrogen soluble index (TCA-NSI) and degree of hydrolysis (DH) of peanut protein hydrolysates (PPH) all reached the highest at 120MPa. Consequently, it possessed the highest angiotensin converting enzyme (ACE) and renin inhibitory activity. The highest surface hydrophobicity occurred at 120 MPa pretreatment samples. Thirty-nine oligopeptides at 120 MPa pretreatment were identified by ultra-performance liquid chromatography-quadrupole time-of-flight (UPLC-Q-TOF) mass spectrometer combined with Progenesis QI for Proteomics software compared with 29 and 35 at control and 210 MPa, respectively. This meant that disaggregation of PPI at 120 MPa resulted in the release of new hydrophobic peptide.
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