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Evaluating Potential Risks of Food Allergy and Toxicity of Soy Leghemoglobin Expressed in Pichia pastoris
Author(s) -
Jin Yuan,
He Xiaoyun,
AndohKumi Kwame,
Fraser Rachel Z.,
Lu Mei,
Goodman Richard E.
Publication year - 2018
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201700297
Subject(s) - pichia pastoris , pichia , biology , toxicity , yeast , pepsin , food science , biochemistry , recombinant dna , chemistry , enzyme , gene , organic chemistry
Scope The Soybean ( Glycine max ) leghemoglobin c2 (LegHb) gene was introduced into Pichia pastoris yeast for sustainable production of a heme‐carrying protein, for organoleptic use in plant‐based meat. The potential allergenicity and toxicity of LegHb and 17 Pichia host‐proteins each representing ≥1% of total protein in production batches are evaluated by literature review, bioinformatics sequence comparisons to known allergens or toxins, and in vitro pepsin digestion. Methods and results Literature searches found no evidence of allergenicity or toxicity for these proteins. There are no significant sequence matches of LegHb to known allergens or toxins. Eleven Pichia proteins have modest identity matches to minor environmental allergens and 13 Pichia proteins have significant matches to proteins from toxic sources. Yet the matched allergens and toxins have similar matches to proteins from the commonly consumed yeast Saccharomyces cerevisiae , without evidence of food allergy or toxicity. The demonstrated history of safe use indicates additional tests for allergenicity and toxicity are not needed. The LegHb and Pichia sp . proteins were rapidly digested by pepsin at pH 2. Conclusion These results demonstrate that foods containing recombinant soy LegHb produced in Pichia sp . are unlikely to present an unacceptable risk of allergenicity or toxicity to consumers.