Safety assessment of glutaminase from <i>Aspergillus niger</i>

Vo, Trung D.; Sulaiman, Christina; Tafazoli, Shahrzad; Lynch, Barry; Roberts, Ashley; Chikamatsu, Go

doi:10.1002/fsn3.1426

Cited by 16 publications

(8 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The "treat-and-wash" method was employed in bacterial reverse mutation tests on other enzymes intended for food production which support the conclusion of a non-mutagenicity of purine nucleosidase under the conditions of this assay. [32][33][34] The lack of genotoxic potential of purine nucleosidase from A. luchuensis was further confirmed in the in vitro mammalian chromosome aberration assay in which no evidence of clastogenic effects were observed up to the highest concentrations tested.…”

Section: Discussionmentioning

confidence: 77%

Safety assessment of purine nucleosidase from Aspergillus luchuensis

Meetro

Floyd

et al. 2021

Toxicology Research and Application

Self Cite

View full text Add to dashboard Cite

Purine nucleosidase (EC 3.2.2.1) catalyzes the N-riboside hydrolysis of purine nucleosides to D-ribose and a purine base. This enzyme may be used in the production of beer and other alcoholic beverages to reduce the purine content of these products. Purine nucleosidase was obtained from Aspergillus luchuensis naturally occurring in grain sources. The safety profile of purine nucleosidase is not well documented in the scientific literature, and a series of toxicological studies were undertaken to investigate the safety of its use in food production. Purine nucleosidase from A. luchuensis was non-mutagenic and non-clastogenic in a standard Ames test and in vitro mammalian chromosome aberration assay. Administration of purine nucleosidase in a 90-day subchronic toxicity study in Sprague-Dawley rats did not elicit adverse findings on any hematology, clinical chemistry, urinalysis, organ weight, or histopathological parameter at doses up to 1700 mg total organic solids (TOS)/kg body weight/day, the highest dose tested. The results suggest purine nucleosidase to lack systemic toxic effect. The no-observed-adverse-effect level was concluded to be 1700 mg TOS/kg body weight/day. The results of the toxicology studies support the safety of purine nucleosidase from a non-genetically modified strain of A. luchuensis when used in food production.

show abstract

Section: Discussionmentioning

confidence: 77%

Safety assessment of purine nucleosidase from Aspergillus luchuensis

Meetro

Floyd

et al. 2021

Toxicology Research and Application

Self Cite

View full text Add to dashboard Cite

show abstract

“…Given that the material is largely proteinaceous, this finding is not surprising and is consistent with the studies of other enzymes produced from other microorganisms, including Aspergillus oryzae and A. niger. 37,38 While the current data support the safety of the β-fructofuranosidase enzyme concentrate produced from A. brunneoviolaceus, it is typical that the safety assessment of enzyme products give consideration to the source organism in addition to the inherent hazard profile of the enzyme. 27,39 No published scientific opinions regarding the safety of A. brunneoviolaceus were identified.…”

Section: Discussionmentioning

confidence: 92%

Safety assessment of β-fructofuranosidase from Aspergillus brunneoviolaceus

Meetro

Lynch

et al. 2021

Toxicology Research and Application

Self Cite

View full text Add to dashboard Cite

β-Fructofuranosidase (β-D-fructofuranoside fructohydrolase; EC 3.2.1.26) is used in the production of fructo-oligosaccharides that are commonly used by the food industry as prebiotics for their purported health benefits. The β-fructofuranosidase discussed herein is obtained from a novel source organism that is a non-genetically modified strain of Aspergillus brunneoviolaceus, which phylogenetically belongs to the Aspergillus section Nigri. The safety of β-fructofuranosidase was evaluated in a series of toxicology studies as prescribed by Tier 1 toxicity testing by the European Food Safety Authority, including an evaluation of the mutagenicity and genotoxicity potential using the in vitro bacterial reverse mutation and mammalian chromosomal aberration assays, as well as systemic toxicity in a 90-day oral subchronic toxicity study in Sprague-Dawley rats. β-Fructofuranosidase was demonstrated to lack mutagenic or genotoxic potential based on the results of the in vitro assays due to absence of increased revertant colonies in the bacterial reverse mutation test and incidence of chromosome aberrations in the chromosomal aberration assay. Administration of β-fructofuranosidase by gavage at doses up to 1200 mg total organic solids (TOS)/kg body weight/day for 90 days did not elicit any systemic toxic effects in rats based on a lack of adverse effect in any study parameter, and therefore the no-observed-adverse-effect level of β-fructofuranosidase was concluded to be 1200 mg TOS/kg body weight/day, the highest dose tested. The results of the toxicology studies on β-fructofuranosidase from A. brunneoviolaceus demonstrate this species to be a safe and suitable source of enzymes for use by the food industry.

show abstract

“…Most microbial L-asparaginases have glutaminase activity, which may cause clinical side effects regarding the use of L-asparaginase as a therapeutic agent. Glutaminase, catalyzing the hydrolytic deamination of L-glutamine to yield L-glutamate and ammonia, has an indirect role in imparting or enhancing the flavor profile of foods by increasing the L-glutamate content of intermediate food ingredients [ 128 ]. Claeys et al reported that the addition of glutamine had a strong promoting effect on acrylamide formation [ 129 ].…”

Section: Discussionmentioning

confidence: 99%

Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives

et al. 2021

View full text Add to dashboard Cite

L-asparaginase (E.C.3.5.1.1) hydrolyzes L-asparagine to L-aspartic acid and ammonia, which has been widely applied in the pharmaceutical and food industries. Microbes have advantages for L-asparaginase production, and there are several commercially available forms of L-asparaginase, all of which are derived from microbes. Generally, L-asparaginase has an optimum pH range of 5.0–9.0 and an optimum temperature of between 30 and 60 °C. However, the optimum temperature of L-asparaginase from hyperthermophilic archaea is considerable higher (between 85 and 100 °C). The native properties of the enzymes can be enhanced by using immobilization techniques. The stability and recyclability of immobilized enzymes makes them more suitable for food applications. This current work describes the classification, catalytic mechanism, production, purification, and immobilization of microbial L-asparaginase, focusing on its application as an effective reducer of acrylamide in fried potato products, bakery products, and coffee. This highlights the prospects of cost-effective L-asparaginase, thermostable L-asparaginase, and immobilized L-asparaginase as good candidates for food application in the future.

show abstract

Safety assessment of glutaminase from Aspergillus niger

Cited by 16 publications

References 17 publications

Safety assessment of purine nucleosidase from Aspergillus luchuensis

Safety assessment of purine nucleosidase from Aspergillus luchuensis

Safety assessment of β-fructofuranosidase from Aspergillus brunneoviolaceus

Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives

Contact Info

Product

Resources

About