Characterization of Penicillium crustosum l-asparaginase and its acrylamide alleviation efficiency in roasted coffee beans at non-cytotoxic levels

Khalil, Neveen M.; Rodríguez‐Couto, Susana; El-Ghany, Mohamed N. Abd

doi:10.1007/s00203-021-02198-6

Cited by 19 publications

(7 citation statements)

References 28 publications

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“…The L-asparaginase-producing bacteria were identified as Stenotrophomonas maltophilia EMCC2297 using 16S rRNA sequencing [ 38 ]. The L-asparaginase-producing fungus was identified as Penicillium crustosum NMKA 511 using nuclear ribosomal DNA ITS sequencing [ 19 ]. The L-asparaginase-producing yeast was identified as Leucosporidium muscorum using 28S rRNA gene sequencing [ 39 ].…”

Section: Sources Of L-asparaginasementioning

confidence: 99%

“…Compared with the control, the acrylamide content of light roasted beans and dark roasted beans treated with the enzyme were reduced to 80.7% and 75.8%, respectively. Furthermore, the amount of L-asparaginase used to reduce acrylamide in roasted coffee beans was considered safe based on the result of a cytotoxicity assay [ 19 ].…”

Section: Application Of Microbial L-asparaginase In Foodmentioning

confidence: 99%

“…Consequently, the European Commission [ 18 ] launched new reduction measures of acrylamide in food in 2017. Operators in the food business in Europe were obliged by Regulation 2158/2017 to reduce acrylamide content in their food products [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

“…Acrylamide mitigation strategies were proposed, such as raw materials selection, product composition alteration, processing conditions optimization, and pretreatment procedures [ 19 ]. Enzymatic treatment, which is a simple and effective way to reduce acrylamide in food without affecting the sensory or nutritional properties of the final product, has been proposed [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

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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.

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Section: Sources Of L-asparaginasementioning

confidence: 99%

Section: Application Of Microbial L-asparaginase In Foodmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

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“…This is of great concern due to its toxicity and widespread presence in thermally processed foods [4]. Various strategies have been used to inhibit the formation of acrylamide, including the careful selection of raw materials, the regulation of processing conditions (temperatures and times), the addition of inhibitors (such as amino acids, organic acids, salts, and glutathione), the addition of plant extracts (phenolics and antioxidants), and the utilization of additives (specific microorganisms and L-asparaginase) [5,6]. Among these approaches, enzymatic treatment is considered to be the simplest and most effective method to inhibit the formation of acrylamide in thermally processed foods without affecting the flavor and nutritional properties of the final product [7].…”

Section: Introductionmentioning

confidence: 99%

Thermal Stability Enhancement of L-Asparaginase from Corynebacterium glutamicum Based on a Semi-Rational Design and Its Effect on Acrylamide Mitigation Capacity in Biscuits

Chi,

Jiang,

Feng

et al. 2023

Foods

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Acrylamide is present in thermally processed foods, and it possesses toxic and carcinogenic properties. L-asparaginases could effectively regulate the formation of acrylamide at the source. However, current L-asparaginases have drawbacks such as poor thermal stability, low catalytic activity, and poor substrate specificity, thereby restricting their utility in the food industry. To address this issue, this study employed consensus design to predict the crucial residues influencing the thermal stability of Corynebacterium glutamicum L-asparaginase (CgASNase). Subsequently, a combination of site-point saturating mutation and combinatorial mutation techniques was applied to generate the double-mutant enzyme L42T/S213N. Remarkably, L42T/S213N displayed significantly enhanced thermal stability without a substantial impact on its enzymatic activity. Notably, its half-life at 40 °C reached an impressive 13.29 ± 0.91 min, surpassing that of CgASNase (3.24 ± 0.23 min). Moreover, the enhanced thermal stability of L42T/S213N can be attributed to an increased positive surface charge and a more symmetrical positive potential, as revealed by three-dimensional structural simulations and structure comparison analyses. To assess the impact of L42T/S213N on acrylamide removal in biscuits, the optimal treatment conditions for acrylamide removal were determined through a combination of one-way and orthogonal tests, with an enzyme dosage of 300 IU/kg flour, an enzyme reaction temperature of 40 °C, and an enzyme reaction time of 30 min. Under these conditions, compared to the control (464.74 ± 6.68 µg/kg), the acrylamide reduction in double-mutant-enzyme-treated biscuits was 85.31%, while the reduction in wild-type-treated biscuits was 68.78%. These results suggest that L42T/S213N is a promising candidate for industrial applications of L-asparaginase.

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Role of Microorganisms in Biodegradation of Pollutants

Fouad¹,

Youssef²,

Shahat³

et al. 2022

Handbook of Biodegradable Materials

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Characterization of Penicillium crustosum l-asparaginase and its acrylamide alleviation efficiency in roasted coffee beans at non-cytotoxic levels

Cited by 19 publications

References 28 publications

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

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

Thermal Stability Enhancement of L-Asparaginase from Corynebacterium glutamicum Based on a Semi-Rational Design and Its Effect on Acrylamide Mitigation Capacity in Biscuits

Role of Microorganisms in Biodegradation of Pollutants

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