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Biochemical Characterization of Thermostable Acrylamide Amidohydrolase from Aspergillus fumigatus with Potential Activity for Acrylamide Degradation in Various Food Products
Faculty
Science
Year:
2024
Type of Publication:
ZU Hosted
Pages:
Authors:
Ashraf Sabry Abdelfattah alsaied
Staff Zu Site
Abstract In Staff Site
Journal:
Current Microbiology Springer
Volume:
Keywords :
Biochemical Characterization , Thermostable Acrylamide Amidohydrolase from Aspergillus
Abstract:
Acrylamide is the major by-product of the Maillard reactions in foods with the overheating processes of L-asparagine-rich foods with reducing sugars that usually allied with neurotoxicity and carcinogenicity. Several approaches have been used to prevent the formation of acrylamide, however, degrading the already formed acrylamide in foods remains unequivocal. Acrylamide hydrolyzing enzyme “amidohydrolase” is one of the most promising enzymes for acrylamide degradation in foods. So, amidohydrolase “amidase” from thermotolerant Aspergillus fumigatus EFBL was purified to their electrophoretic homogeneity by gel-filtration and ion-exchange chromatography, with overall purification folds 2.8 and yield 9.43%. The apparent molecular subunit structure of the purified A. fumigatus amidase was 50 kDa, with highest activity at reaction temperature of 40 °C and pH of 7.5 The enzyme displayed a significant thermal stability as revealed from the value of T1/2 (13.37 h), and thermal denaturation rate (Kr 0.832 × 10– 3 min) at 50 °C, with metalloproteinic identity. The purified enzyme had a significant activity for acrylamide degradation in various food products such as meat, cookies, potato chips, and bread as revealed from the HPLC analysis and LC–MS analysis. So, with the purified amidase, the acrylamide in the food products was degraded by about 95% to acrylic acid, ensuring the possibility of using this enzyme in abolishing the toxic acrylamide in the foods products. This is the first report exploring the potency of A. fumigatus amidase for an actual degradation of acrylamide in foods efficiently. Further biochemical analyses are ongoing to assess the affinity of this enzyme for selective hydrolyses of acrylamide in foods, without affecting the beneficial stereochemical related compounds.
Author Related Publications
Ashraf Sabry Abdelfattah alsaied, "Characterization of Homocysteine γ-Lyase from Submerged and Solid Cultures of Aspergillus fumigatus ASH (JX006238)", Korean Society of Microbiology and Biotechnology, 2013
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Ashraf Sabry Abdelfattah alsaied, "Purification and Characterization of LAmino Acid Oxidase from the SolidState Grown Cultures of Aspergillus oryzae ASH1", Pleiades Publishing, LTD, 2013
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Ashraf Sabry Abdelfattah alsaied, "Microbial L-methioninase: production, molecular characterization, and therapeutic applications", Springer-Verlag 2010, 2010
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Ashraf Sabry Abdelfattah alsaied, "Characterization and immobilization of purified Aspergillus flavipes L-methioninase: continuous production of methanethiol", The Society of Applied Microbiology, 2011
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Ashraf Sabry Abdelfattah alsaied, "L-methioninase production by Aspergillus flavipes under solid-state fermentation", Wiley-VCH Verlag GmbH and Co. KGaA, Weinheim, 2009
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Department Related Publications
Gamal abdelaziz abdelhamid, "Characterization and identification of multidrug resistant bacteria from some Egyptian patients", Asian Network for Scientific Information,Science Alert ISSN 1682-296x, 2013
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Fifi Mohamed Reda Mohamed, "Sorption of cadmium and lead ions by Cunninghamella elagens lender ML2. Egyptian J. of Microbiology", Egypt, 2011
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Gamal abdelaziz abdelhamid, "coliphages lysing Escherichia coli bactertia: their morphology and their response to some physical factors", Medwell Journals Scientific Research Publishing Company, 2013
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Manal Tawfiq Ibrahim, "CHANGES IN POLYAMINES IN TOMATO PLANTS AND IN CULTURED TOMATO TISSUES INFECTED WITH PSEUDOMONAS SYRINGAE PV. TOMATO", national research center, 2010
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Ashraf Sabry Abdelfattah alsaied, "L-Amino Acid Oxidase from Filamentous Fungi: Screening and Optimization.", Springer-Verlag and the University of Milan 2011, 2012
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