Bioactive hydrolysates from bovine blood globulins: Generation, characterisation, and in silico prediction of toxicity and allergenicity

被引:36
作者
Lafarga, Tomas [1 ]
Wilm, Matthias [2 ]
Wynne, Kieran [2 ]
Hayes, Maria [1 ]
机构
[1] TEAGASC, Food BioSci Dept, Irish Agr & Food Dev Author, Dublin 15, Ireland
[2] Univ Coll Dublin, Conway Inst, Dublin 4, Ireland
关键词
Bovine blood proteins; ACE-I; Allergenicity; In silico analysis; Functional ingredients; Bioinformatics; DIPEPTIDYL-PEPTIDASE-IV; FUNCTIONAL-PROPERTIES; INHIBITORY PEPTIDES; BEEF ALLERGY; MEAT; PROTEINS; IDENTIFICATION; IGE; PRODUCTS; SAFETY;
D O I
10.1016/j.jff.2016.03.031
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Two protein fractions rich in gamma-globulins (FI) and alpha- and beta-globulins (FII) were generated from bovine blood and hydrolysed with the enzyme papain. The generated hydrolysates showed in vitro angiotensin-I-converting enzyme (ACE-I), renin, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. A total of 626 and 2246 peptides were identified by LC-MS/MS from the 1 kDa fractions of FI and FII, and the potential toxicity and allergenicity of these peptides were assessed in silico using three independent predictive approaches. All of the peptides identified from the bioactive blood protein fractions FI and FII were predicted to be nontoxic. However, 72 peptides from FI and 492 peptides from FII were identified as potential allergens with at least two predictive approaches. Results suggested that papain hydrolysates of FI and FII contain potential allergenic peptides, and those products containing such hydrolysates should be labelled correctly in line with Food and Consumer legislation Regulation (EU) No.1169/2011. (c) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:142 / 155
页数:14
相关论文
共 58 条
[11]   Isolation and characterization of a heat-resistant beef allergen:: myoglobin [J].
Fuentes, MM ;
Palacios, R ;
Garcés, MM ;
Caballero, ML ;
Moneo, I .
ALLERGY, 2004, 59 (03) :327-331
[12]   ExPASy: the proteomics server for in-depth protein knowledge and analysis [J].
Gasteiger, E ;
Gattiker, A ;
Hoogland, C ;
Ivanyi, I ;
Appel, RD ;
Bairoch, A .
NUCLEIC ACIDS RESEARCH, 2003, 31 (13) :3784-3788
[13]  
GUPTA S, 2013, PLOS ONE, V8, DOI [10.1371/JOURNAL.PONE.0073957, DOI 10.1371/JOURNAL.PONE.0073957]
[14]   Identification of galactose-α-1,3-galactose in the gastrointestinal tract of the tick Ixode sricinus; possible relationship with red meat allergy [J].
Hamsten, C. ;
Starkhammar, M. ;
Tran, T. A. T. ;
Johansson, M. ;
Bengtsson, U. ;
Ahlen, G. ;
Sallberg, M. ;
Gronlund, H. ;
van Hage, M. .
ALLERGY, 2013, 68 (04) :549-552
[15]   Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates [J].
He, Rong ;
Alashi, Adeola ;
Malomo, Sunday A. ;
Girgih, Abraham T. ;
Chao, Dongfang ;
Ju, Xingrong ;
Aluko, Rotimi E. .
FOOD CHEMISTRY, 2013, 141 (01) :153-159
[16]   Meat allergy [J].
Hemmer, W. ;
Mayer, D. ;
Jarisch, R. .
ALLERGOLOGIE, 2011, 34 (08) :373-387
[17]   Hypoallergenic formulas - when, to whom and how long: after more than 15 years we know the right indication! [J].
Host, A ;
Halken, S .
ALLERGY, 2004, 59 :45-52
[18]   Utilization of bovine blood plasma proteins for the production of angiotensin I converting enzyme inhibitory peptides [J].
Hyun, CK ;
Shin, HK .
PROCESS BIOCHEMISTRY, 2000, 36 (1-2) :65-71
[19]   High-performance size-exclusion chromatography of peptides [J].
Irvine, GB .
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 2003, 56 (1-3) :233-242
[20]   Melittin peptides exhibit different activity on different cells and model membranes [J].
Jamasbi, Elaheh ;
Batinovic, Steven ;
Sharples, Robyn A. ;
Sani, Marc-Antoine ;
Robins-Browne, Roy Michael ;
Wade, John D. ;
Separovic, Frances ;
Hossain, Mohammed Akhter .
AMINO ACIDS, 2014, 46 (12) :2759-2766