TY - JOUR
T1 - Effects of Low-pH Treatment on the Allergenicity Reduction of Black Turtle Bean (Phaseolus vulgaris L.) Lectin and Its Mechanism
AU - He, Shudong
AU - Zhao, Jinlong
AU - Zhang, Yi
AU - Zhu, Yuchen
AU - Li, Xingjiang
AU - Cao, Xiaodong
AU - Ye, Yongkang
AU - Li, Jing
AU - Sun, Hanju
N1 - Funding Information:
The authors are grateful for the financial support from the National Natural Science Foundation of China (Grant No. 31701524).
Publisher Copyright:
©
PY - 2021/2/3
Y1 - 2021/2/3
N2 - A high content of potentially allergenic lectin in Phaseolus vulgaris L. beans is of increasing health concerns; however, understanding of the protein allergenicity mechanism on the molecular basis is scarce. In the present study, low-pH treatments were applied to modify black turtle bean lectin allergen, and a sensitization procedure was performed using the BALB/c mice for the allergenicity evaluation, while the conformational changes were monitored by the spectral analyses and the details were explored by the molecular dynamics simulation. Much milder anaphylactic responses were observed in BALB/c mice experiments. At the molecular level, the protein was unfolded in low acidic environments because of protonation, and α-helix was reduced with the exposure of trypsin cleavage sites, especially the improvement of protease accessibility for Lys121, 134, and 157 in the B cell epitope structural alterations. These results indicate that a low-pH treatment might be an efficient method to improve the safety of legume protein consumption.
AB - A high content of potentially allergenic lectin in Phaseolus vulgaris L. beans is of increasing health concerns; however, understanding of the protein allergenicity mechanism on the molecular basis is scarce. In the present study, low-pH treatments were applied to modify black turtle bean lectin allergen, and a sensitization procedure was performed using the BALB/c mice for the allergenicity evaluation, while the conformational changes were monitored by the spectral analyses and the details were explored by the molecular dynamics simulation. Much milder anaphylactic responses were observed in BALB/c mice experiments. At the molecular level, the protein was unfolded in low acidic environments because of protonation, and α-helix was reduced with the exposure of trypsin cleavage sites, especially the improvement of protease accessibility for Lys121, 134, and 157 in the B cell epitope structural alterations. These results indicate that a low-pH treatment might be an efficient method to improve the safety of legume protein consumption.
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U2 - 10.1021/acs.jafc.0c06524
DO - 10.1021/acs.jafc.0c06524
M3 - Article
C2 - 33464885
AN - SCOPUS:85100233945
SN - 0021-8561
VL - 69
SP - 1379
EP - 1390
JO - Journal of agricultural and food chemistry
JF - Journal of agricultural and food chemistry
IS - 4
ER -