Safety evaluation of nuclease P1 from Penicillium citrinum

Okado, Nobuo; Hasegawa, Kazushige; Mizuhashi, Fukutaro; Lynch, Barry; Vo, Trung D.; Roberts, Ashley

doi:10.1016/j.fct.2015.12.001

Cited by 13 publications

(10 citation statements)

References 13 publications

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“…Additionally, amino acids released during the incubation can be associated with overgrowth of nonrevertant background lawn bacteria, which also limits the interpretability of the results (EFSA, 2014;Thompson et al, 2005). Similar increases in the number of revertants, which also were considered as likely due to the copresence of free amino acids, were reported in another Ames assay with a different enzyme preparation (enzymes nuclease P1 from Penicillium citrium) when testing was conducted under preincubation conditions (Okado et al, 2016). Similar increases in the number of revertants, which also were considered as likely due to the copresence of free amino acids, were reported in another Ames assay with a different enzyme preparation (enzymes nuclease P1 from Penicillium citrium) when testing was conducted under preincubation conditions (Okado et al, 2016).…”

Section: In Vivo Comet Testmentioning

confidence: 87%

“…In such instances, the treat-and-wash protocol in which bacteria are washed after treatment with the test article to remove free amino acids is considered as an acceptable modification of the preincubation method (EFSA, 2014; Thompson et al, 2005). Similar increases in the number of revertants, which also were considered as likely due to the copresence of free amino acids, were reported in another Ames assay with a different enzyme preparation (enzymes nuclease P1 from Penicillium citrium) when testing was conducted under preincubation conditions (Okado et al, 2016). When testing was repeated using the treat-and-wash method, an increase in revertant colonies was not observed in any of the tester strains, and thus, P. citrium-derived nuclease P1 was concluded to be nonmutagenic.…”

Section: In Vivo Comet Testmentioning

confidence: 88%

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Safety evaluation of arabinase (arabinan endo‐1,5‐α‐L‐arabinanase) from Aspergillus tubingensis

Okado

Sugi²,

Kasamoto³

et al. 2019

Food Science & Nutrition

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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.

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Section: In Vivo Comet Testmentioning

confidence: 87%

Section: In Vivo Comet Testmentioning

confidence: 88%

Safety evaluation of arabinase (arabinan endo‐1,5‐α‐L‐arabinanase) from Aspergillus tubingensis

Okado

Sugi²,

Kasamoto³

et al. 2019

Food Science & Nutrition

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“…Nuclease P1 from P . citrinum , an anamorphic mesophilic fungus with a history of safe use as a fermentation organism in Europe and Asia, is used in the production of ribonucleases [ 25 ]; however, the safety of 5′-PDE from A . fumigatus , a pathogenic bacteria, for use in food processing should be comprehensively evaluated by means of standard toxicological testing methods, including in vitro Ames tests and chromosome-aberration assays and in vivo rat erythrocyte micronucleus assays, in future studies.…”

Section: Discussionmentioning

confidence: 99%

Isolation, purification and characterization of 5'-phosphodiesterase from Aspergillus fumigatus

Luo

Fan

et al. 2017

PLoS ONE

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5′-Phosphodiesterase (5′-PDE) catalyzes the hydrolysis of ribonucleic acid to obtain a mixture of ribonucleotides, such as 5′-guanosine monophosphate and 5′-adenosine monophosphate. In this study, a 5'-PDE was newly isolated and purified from Aspergillus fumigatus. Following purification, this enzyme exhibited a specific activity of 1036.76 U/mg protein, a molecular weight of 9.5 kDa, and an optimal temperature and pH for enzyme activity of 60°C and 5.0, respectively. However, its activity was partially inhibited by Fe3+, Cu2+, and Zn2+, but slightly improved by the presence of K+ and Na+. Additionally, chemical-modification experiments were also applied to investigate the structural information of 5'-PDE, in which the residues containing carboxyl and imidazole groups were essential for enzyme activity based on their localization in the 5′-PDE active site. Furthermore, purified 5′-PDE could specifically catalyze the synthesis of ribonucleotides with a Vmax 0.71 mmol/mg·min and a KM of 13.60 mg/mL.

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“…Barley rootlets are good source of this enzyme among others including deoxyribonuclease, ribonuclease and adenosine-5'-phosphomono-esterase. As previously mentioned, this enzyme can be obtained from a variety of other sources such as plant (Beluhan et al, 2020), animal (Cesarini et al, 2020) and microbial (Okado et al, 2016). However, considering economic aspects, preparations of 5'-PDE from a cheap source residue such malt roots is very promising.…”

Section: Introductionmentioning

confidence: 99%

5'-Ribonucleotides production using 5'-phosphodiesterase from spent malt roots

Alves

Souza

Macieja

et al. 2021

Braz. J. Food Technol.

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5'-ribonucleotides are high value-added molecules widely used in the food and pharmaceutical industries because of their bioactive properties. The present work aims to produce a composition of 5’-ribonucleotides using spent brewer’s yeast as cheap source of RNA, and barley malt rootlets as cheap source of 5'-phosphodiesterase (5'-PDE). This is a very promising and innovative strategy because both spent yeast and malt rootles are residues of the brewing process and are closely linked in a cycle that until now is not yet commercially exploited due to lack of studies. Our results showed that extraction of 5’-PDE was mainly influenced by the fineness of the rootlets and amount of extraction solvent (water). The main molecules formed during RNA hydrolysis were 5’-ribonucleotides, which represented 85.86% of the total hydrolyzed molecules. Finally, the results of the proposed approach can generate a new perspective for the brewing industry regarding the management of its wastes, generating from them products of high added value and with a wide range of applications.

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Safety evaluation of nuclease P1 from Penicillium citrinum

Cited by 13 publications

References 13 publications

Safety evaluation of arabinase (arabinan endo‐1,5‐α‐L‐arabinanase) from Aspergillus tubingensis

Safety evaluation of arabinase (arabinan endo‐1,5‐α‐L‐arabinanase) from Aspergillus tubingensis

Isolation, purification and characterization of 5'-phosphodiesterase from Aspergillus fumigatus

5'-Ribonucleotides production using 5'-phosphodiesterase from spent malt roots

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