Analysis of α-helix unfolding in the pine nut peptide Lys-Cys-His-Lys-Pro induced by pulsed electric field

2017 ◽  
Vol 97 (12) ◽  
pp. 4058-4065 ◽  
Author(s):  
Jie Xing ◽  
Sitian Zhang ◽  
Mingdi Zhang ◽  
Songyi Lin
LWT ◽  
2017 ◽  
Vol 75 ◽  
pp. 366-372 ◽  
Author(s):  
Songyi Lin ◽  
Rong Liang ◽  
Peiyu Xue ◽  
Shuyu Zhang ◽  
Zeyu Liu ◽  
...  

Author(s):  
Songyi Lin ◽  
Rong Liang ◽  
Jie Xing ◽  
Xingfang Li ◽  
Yali Yu ◽  
...  

Abstract The purpose of the study was to evaluate the relationship between antioxidant activity improvement and structure changes of peptide (Ser-His-Glu-Cys-Asn (SHECN) isolated from soybean treated by pulsed electric field (PEF). The two-factor-at-a–time (TFAT) was performed to investigate interaction of electric field intensity (5, 10, 15 and 20 kV/cm) and pulse frequency (1,800 and 2,400 Hz) on antioxidant activity improvement and structure changes. Compared with untreated peptide, DPPH radical inhibition of SHECN was significantly increased to 95.54 ± 0.16 % at optimal conditions (electric field intensity 15 kV/cm, pulse frequency 1,800 Hz and a retention time of 2 h). Results showed that the primary structure of SHECN had not been changed based on the nuclear magnetic resonance analysis. However, the secondary structure of peptide, especially α-helix can be changed. These results suggested that mechanism of antioxidant activity improvement is related to secondary structure changes.


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