Abstract
Arabinase is an enzyme recognized for its ability to degrade arabinan, a plant cell wall constituent. It has been applied in the food industry most commonly for juice processing. One commercial source of arabinase is Aspergillus tubingensis (A. tubingensis), a black Aspergillus species. Given the intended use in food for human consumption, and noting its potential presence at trace levels in finished products, a series of safety studies including in vitro Ames and chromosome aberration assays, in vivo mammalian erythrocyte micronucleus and alkaline comet assays, and a 90‐day rat oral toxicity study were conducted. No test article‐related mutagenic activity was observed in the Ames assay. Although positive activity was observed in the chromosome aberration assay, this was not replicated in the in vivo genotoxicity assays including in preabsorptive cells. In the subchronic toxicity study, no test article‐related adverse effects were observed following oral administration of arabinase at doses of 15.3, 153, or 1,530 mg total organic solids (TOS)/kg body weight/day to Sprague Dawley rats. The no‐observed‐adverse‐effect level was considered to be the highest dose tested (1,530 mg TOS/kg body weight/day). The results of the genotoxicity studies and the subchronic toxicity study support the safe use of arabinase from A. tubingensis in food production.
Highlights
Arabinase (5-α-L-arabinan 5-α-L-arabinanohydrolase; arabinan endo-1,5-α-L-arabinanase; EC 3.2.1.99), referred to as arabanase or arabinanase, is a well-characterized enzyme that catalyzes the endohydrolysis of (1 → 5)-α-arabinofuranosidic linkages in polysaccharides of arabinose (BRENDA Professional, 2018)
Arabinase is typically used in fruit juice processing, in the production of apple and pear juices, for its ability to break down arabinans, the formation of which is responsible for fruit juice cloudiness (Aehle, 2007; Bayindirli, 2010; Sharma, Patel, & Sharma, 2014; Voragen, Rombouts, Searle-van Leeuwen, Schols, & Pilnik, 1987)
Arabinase acts to clarify juice by degrading arabinose polymers, the presence of which is associated with juice cloudiness or haze
Summary
A. tubingensis, and ascertain this Aspergillus species as a safe source for a food enzyme, key toxicity assessments were conducted in accordance with current study guidelines. The objective of the present study was to evaluate the safety of arabinase derived from a nongenetically modified A. tubingensis strain GPA41 (hereinafter referred to as AG) for use in food processing. To this end, AG, in the form of an ultrafiltered concentrate, was subjected to a standard battery of toxicological testing, consisting of a 90-day repeated oral dose toxicity test conducted in rats and a series of in vitro and in vivo genotoxicity tests. The potential of AG concentrate to induce DNA damage was further examined in an in vivo comet assay conducted in rats
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