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Evaluating the Potential for Enzymatic Acrylamide Mitigation in a Range of Food Products Using an Asparaginase from Aspergillus oryzae
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/geno.1997.4995openalex-snapshot
Comparison of DNA Sequences with Protein Sequences
inferredcites →https://doi.org/10.1007/s00003-006-0005-6openalex-snapshot
Dietary Acrylamide and Cancer Risk in Humans: A Review
inferredcites →https://doi.org/10.1016/j.aca.2004.03.086openalex-snapshot
Analysis of acrylamide in different foodstuffs using liquid chromatography–tandem mass spectrometry and gas chromatography–tandem mass spectrometry
inferredcites →https://doi.org/10.1016/j.foodchem.2004.05.050openalex-snapshot
Influence of variety and processing conditions on acrylamide levels in fried potato crisps
inferredcites →https://doi.org/10.1016/j.foodchem.2007.07.001openalex-snapshot
Impact of chemical pre-treatments on the acrylamide formation and sensorial quality of potato crisps
inferredcites →https://doi.org/10.1016/j.foodchem.2007.12.057openalex-snapshot
The effect of asparaginase on acrylamide formation in French fries
inferredcites →https://doi.org/10.1016/j.jcs.2007.06.016openalex-snapshot
Acrylamide in cereal products: A review
inferredcites →https://doi.org/10.1016/j.jfoodeng.2006.04.014openalex-snapshot
Acrylamide reduction under different pre-treatments in French fries
inferredcites →https://doi.org/10.1016/s0021-9258(18)37878-5openalex-snapshot
Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene.
inferredcites →https://doi.org/10.1021/jf0261506openalex-snapshot
Why Asparagine Needs Carbohydrates To Generate Acrylamide
inferredcites →https://doi.org/10.1021/jf034180iopenalex-snapshot
Acrylamide Formation Mechanism in Heated Foods
inferredcites →https://doi.org/10.1021/jf034344vopenalex-snapshot
Potential of Acrylamide Formation, Sugars, and Free Asparagine in Potatoes: A Comparison of Cultivars and Farming Systems
inferredcites →https://doi.org/10.1021/jf0349376openalex-snapshot
Acrylamide in French Fries: Influence of Free Amino Acids and Sugars
inferredcites →https://doi.org/10.1021/jf048082oopenalex-snapshot
Addition of Glycine Reduces the Content of Acrylamide in Cereal and Potato Products
inferredcites →https://doi.org/10.1021/jf048557bopenalex-snapshot
Measurement of Acrylamide and Its Precursors in Potato, Wheat, and Rye Model Systems
inferredcites →https://doi.org/10.1021/jf049269iopenalex-snapshot
Effective Ways of Decreasing Acrylamide Content in Potato Crisps during Processing
inferredcites →https://doi.org/10.1021/jf049648bopenalex-snapshot
Acrylamide in Gingerbread: Critical Factors for Formation and Possible Ways for Reduction
inferredcites →https://doi.org/10.1038/419448aopenalex-snapshot
Acrylamide is formed in the Maillard reaction
inferredcites →https://doi.org/10.1038/419449aopenalex-snapshot
Acrylamide from Maillard reaction products
inferredcites →https://doi.org/10.1038/nbt1288-1419openalex-snapshot
High Level Expression of Recombinant Genes in Aspergillus Oryzae
inferredcites →https://doi.org/10.1080/02652030701242558openalex-snapshot
Occurrence of acrylamide in selected foods and mitigation options
inferredcites →https://doi.org/10.1080/110264802762225273openalex-snapshot
Acrylamide in food: mechanisms of formation and influencing factors during heating of foods
inferredcites →https://doi.org/10.1111/j.1753-4887.2004.tb00018.xopenalex-snapshot
Acrylamide: An Update on Current Knowledge in Analysis, Levels in Food, Mechanisms of Formation, and Potential Strategies of Control
inferredcites →https://doi.org/10.1385/1-59259-192-2:185openalex-snapshot
Flexible Sequence Similarity Searching with the FASTA3 Program Package
inferredcites →https://doi.org/10.17221/10603-cjfsopenalex-snapshot
Ways to reduce the acrylamide formation in cracker products
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4837114openalex-extracted
Evaluation of the Effect of Enzymatic Pretreatment with L-Asparaginase on Acrylamide Formation During Microwave, Air and Deep Frying of Potatoes
inferred← citeshttps://doi.org/10.1002/bab.1888openalex-snapshot
A comprehensive review on microbial l ‐asparaginase: Bioprocessing, characterization, and industrial applications
inferred← citeshttps://doi.org/10.1002/cem.3024openalex-snapshot
Process‐centric and data‐centric strategies for enhanced production of l ‐asparaginase—an anticancer enzyme, using marine‐derived Aspergillus niger
inferred← citeshttps://doi.org/10.1002/cphc.201700339openalex-snapshot
Protocol for Computational Enzymatic Reactivity Based on Geometry Optimisation
inferred← citeshttps://doi.org/10.1002/ejlt.201300281openalex-snapshot
Acrylamide – Still a matter of concern for fried potato food?*
inferred← citeshttps://doi.org/10.1002/elsc.201800166openalex-snapshot
Design of a high‐efficiency synthetic system for l ‐asparaginase production in Bacillus subtilis
inferred← citeshttps://doi.org/10.1002/jobm.201300741openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/jsfa.6349openalex-snapshot
Current issues in dietary acrylamide: formation, mitigation and risk assessment
inferred← citeshttps://doi.org/10.1007/978-3-030-10480-1_15openalex-snapshot
Marine Fungal White Biotechnology: An Ecological and Industrial Perspective
inferred← citeshttps://doi.org/10.1007/978-3-319-48665-9_5openalex-snapshot
Blanching as an Acrylamide Mitigation Technique
inferred← citeshttps://doi.org/10.1007/978-981-10-8064-7_10openalex-snapshot
Fungal Endophytes from Anticancer Plants as Producers of the Antitumor Agent L-Asparaginase: A Look at Diversity, Ubiquity, and Enzyme Production
inferred← citeshttps://doi.org/10.1007/978-981-13-3263-0_14openalex-snapshot
Digestive Enzymes: Industrial Applications in Food Products
inferred← citeshttps://doi.org/10.1007/978-981-13-3263-0_5openalex-snapshot
Recent Development in the Uses of Asparaginase as Food Enzyme
inferred← citeshttps://doi.org/10.1007/978-981-13-3263-0_6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-981-16-5214-1_8openalex-snapshot
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l-Asparaginase and Methioninase as Prospective Anticancer Enzymes: Current Applications and Production Approaches
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Raising agents strongly influence acrylamide and HMF formation in cookies and conditions for asparaginase activity in dough
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Enhanced extracellular production of L-asparaginase from Bacillus subtilis 168 by B. subtilis WB600 through a combined strategy
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inferred← citeshttps://doi.org/10.1007/s00253-021-11359-yopenalex-snapshot
L-asparaginase production review: bioprocess design and biochemical characteristics
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inferred← citeshttps://doi.org/10.1007/s10123-024-00493-yopenalex-snapshot
Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis
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Production of a Novel Marine Pseudomonas aeruginosa Recombinant L-Asparaginase: Insight on the Structure and Biochemical Characterization
inferred← citeshttps://doi.org/10.1007/s10529-017-2470-7openalex-snapshot
Characterization of a novel asparaginase from soil metagenomic libraries generated from forest soil
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Penicillium and Talaromyces endophytes from Tillandsia catimbauensis, a bromeliad endemic in the Brazilian tropical dry forest, and their potential for l-asparaginase production
inferred← citeshttps://doi.org/10.1007/s11274-022-03420-3openalex-snapshot
Cacti as low-cost substrates to produce L-asparaginase by endophytic fungi
inferred← citeshttps://doi.org/10.1007/s11274-025-04614-1openalex-snapshot
L-asparaginase: a review of microbial production and protein engineering with translational applications for oncology and food safety
inferred← citeshttps://doi.org/10.1007/s11356-023-26977-4openalex-snapshot
Synergistic effects of ternary mixture formulation and process parameters optimization in a sequential approach for enhanced L-asparaginase production using agro-industrial wastes
inferred← citeshttps://doi.org/10.1007/s11756-024-01624-6openalex-snapshot
Biochemical characterization of genome derived L-asparaginase from eurypsychrophilic Iodobacter sp. PCH194 for therapeutic and food applications
inferred← citeshttps://doi.org/10.1007/s11756-024-01801-7openalex-snapshot
Looking into the thermostable archaeal l-asparaginases
inferred← citeshttps://doi.org/10.1007/s12010-015-1917-3openalex-snapshot
A Comprehensive Review on l-Asparaginase and Its Applications
inferred← citeshttps://doi.org/10.1007/s12010-016-2345-8openalex-snapshot
Isolation and Characterization of Acrylamidase from Arthrobacter sp. DBV1 and Its Ability to Biodegrade Acrylamide
inferred← citeshttps://doi.org/10.1007/s12230-013-9321-4openalex-snapshot
Acrylamide in Processed Potato Products
inferred← citeshttps://doi.org/10.1007/s12257-019-0147-xopenalex-snapshot
Production of Recombinant Human Asparaginase from Escherichia coli under Optimized Fermentation Conditions: Effect of Physicochemical Properties on Enzyme Activity
inferred← citeshttps://doi.org/10.1007/s12268-011-0053-zopenalex-snapshot
Bedeutung der Biotechnologie in der Lebensmittelproduktion
inferred← citeshttps://doi.org/10.1007/s12649-020-01208-wopenalex-snapshot
Enzymatic Technology Application on Coffee Co-products: A Review
inferred← citeshttps://doi.org/10.1007/s13205-014-0215-zopenalex-snapshot
Combination of environmental stress and localization of l-asparaginase in Arthrospira platensis for production improvement
inferred← citeshttps://doi.org/10.1007/s13205-015-0278-5openalex-snapshot
Effective treatment for suppression of acrylamide formation in fried potato chips using L-asparaginase from Bacillus subtilis
inferred← citeshttps://doi.org/10.1007/s13205-019-1814-5openalex-snapshot
l-Asparaginase from Aspergillus spp.: production based on kinetics, thermal stability and biochemical characterization
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Apoptosis induction in leukemic cells by L-asparaginase preparation from Bacillus indicus: bench-scale production, purification and therapeutic application
inferred← citeshttps://doi.org/10.1007/s40011-021-01234-1openalex-snapshot
Statistical Optimization of Bioprocess Parameters for Improved Production of L-Asparaginase from Lactobacillus plantarum
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inferred← citeshttps://doi.org/10.1007/s43393-026-00533-wopenalex-snapshot
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Glutaminase free L-asparaginase from seaweed associated Bacillus licheniformis with promising therapeutic potential
inferred← citeshttps://doi.org/10.1016/b978-0-08-100596-5.22827-8openalex-snapshot
Mitigation of Acrylamide in Thermally Processed Foods
inferred← citeshttps://doi.org/10.1016/b978-0-08-100722-8.00014-0openalex-snapshot
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Fortification with Free Amino Acids Affects Acrylamide Content in Yeast Leavened Bread
inferred← citeshttps://doi.org/10.1016/b978-0-12-800002-1.00018-2openalex-snapshot
Acrylamide in Potato Products
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Impact of l-Asparaginase on Acrylamide Content in Fried Potato and Bakery Products
inferred← citeshttps://doi.org/10.1016/b978-0-12-813280-7.00016-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-12-817380-0.00010-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-12-819820-9.00015-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-12-821005-5.00015-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-12-822945-3.00022-1openalex-snapshot
l-Asparaginases from hyperthermophilic archaea and their applications
inferred← citeshttps://doi.org/10.1016/b978-0-323-99119-3.00021-7openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-443-13263-6.00004-3openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/bs.afnr.2016.05.003openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.afres.2025.101237openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2016.02.006openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2018.01.004openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2018.11.018openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2019.101377openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2023.102977openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bcab.2025.103833openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.biortech.2018.04.012openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bjm.2016.10.004openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.chroma.2021.462746openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.chroma.2023.463938openalex-snapshot
Continuous protein refolding and purification by two-stage periodic counter-current chromatography
inferred← citeshttps://doi.org/10.1016/j.cofs.2014.09.004openalex-snapshot
Enzymatic prevention of health risks in food
inferred← citeshttps://doi.org/10.1016/j.ejar.2015.10.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.enzmictec.2015.08.009openalex-snapshot
Amino acid residues adjacent to the catalytic cavity of tetramer l-asparaginase II contribute significantly to its catalytic efficiency and thermostability
inferred← citeshttps://doi.org/10.1016/j.fct.2014.03.037openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.focha.2023.100206openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.fochx.2024.102055openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.fochx.2025.102605openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2010.11.007openalex-snapshot
Modelling the effect of asparaginase in reducing acrylamide formation in biscuits
inferred← citeshttps://doi.org/10.1016/j.foodchem.2011.08.001openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2016.04.105openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2019.05.171openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2020.126771openalex-snapshot
Exposure of the Croatian adult population to acrylamide through bread and bakery products
inferred← citeshttps://doi.org/10.1016/j.foodchem.2020.128045openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.130046openalex-snapshot
Efficient control of acrylamide in French fries by an extraordinarily active and thermo-stable l-asparaginase: A lab-scale study
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.134224openalex-snapshot
Effectiveness of asparaginase on reducing acrylamide formation in bakery products according to their dough type and properties
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.146194openalex-snapshot
The microbial approach for mitigation of acrylamide in processed foods: A critical review
inferred← citeshttps://doi.org/10.1016/j.foodchem.2026.148843openalex-snapshot
Utilization of enzymes for improving fried flour products: Recent advances, applications, and regulations
inferred← citeshttps://doi.org/10.1016/j.foodcont.2012.07.012openalex-snapshot
Study on the reduction of acrylamide in mixed rye bread by fermentation with bacteriocin-like inhibitory substances producing lactic acid bacteria in combination with Aspergillus niger glucoamylase
inferred← citeshttps://doi.org/10.1016/j.foodcont.2024.110484openalex-snapshot
Acrylamide in coffee: Strategies, research and future perspectives
inferred← citeshttps://doi.org/10.1016/j.foodres.2011.06.025openalex-snapshot
Effect of formulation on the capacity of l-asparaginase to minimize acrylamide formation in short dough biscuits
inferred← citeshttps://doi.org/10.1016/j.foodres.2015.08.031openalex-snapshot
Biochemical characterization of a novel l-asparaginase from Bacillus megaterium H-1 and its application in French fries
inferred← citeshttps://doi.org/10.1016/j.foodres.2019.108658openalex-snapshot
Fungal L-asparaginase: Strategies for production and food applications
inferred← citeshttps://doi.org/10.1016/j.foodres.2022.111936openalex-snapshot
Acrylamide mitigation in foods using recombinant L-asparaginase: An extremozyme from Himalayan Pseudomonas sp. PCH182
inferred← citeshttps://doi.org/10.1016/j.foodres.2023.113177openalex-snapshot
Effective mitigation in the amount of acrylamide through enzymatic approaches
inferred← citeshttps://doi.org/10.1016/j.foodres.2024.114333openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e31790openalex-snapshot
Pulsed electric field effect on acrylamide reduction and quality attributes of continuous-style Lamoka potato chips
inferred← citeshttps://doi.org/10.1016/j.ifset.2014.05.002openalex-snapshot
Mitigation of acrylamide and hydroxymethylfurfural in biscuits using a combined partial conventional baking and vacuum post-baking process: Preliminary study at the lab scale
inferred← citeshttps://doi.org/10.1016/j.ifset.2020.102310openalex-snapshot
A novel strategy of acrylamide mitigation in fried potatoes using asparaginase and high pressure technology
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.07.031openalex-snapshot
A novel bacterial type II l -asparaginase and evaluation of its enzymatic acrylamide reduction in French fries
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.11.115openalex-snapshot
Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2017.11.114openalex-snapshot
Characterization of L-asparaginase from marine-derived Aspergillus niger AKV-MKBU, its antiproliferative activity and bench scale production using industrial waste
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.09.015openalex-snapshot
Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.09.162openalex-snapshot
Characterization of a novel and glutaminase-free type II L-asparaginase from Corynebacterium glutamicum and its acrylamide alleviation efficiency in potato chips
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.128576openalex-snapshot
Biochemical characterization of glutaminase-free L-asparaginases from Himalayan Pseudomonas and Rahnella spp. for acrylamide mitigation
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.147259openalex-snapshot
Immobilization and SPR-based binding characterization of L-asparaginase on metal-chelated polymeric nanoparticles
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.150819openalex-snapshot
Biochemical insights into the key residue substituents of an L-asparaginase from Thermococcus kodakarensis and their application in acrylamide mitigation
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.154669openalex-snapshot
Comprehensive structural and functional characterization of class 3 L-asparaginases from selected pathogenic fungi
inferred← citeshttps://doi.org/10.1016/j.ijfoodmicro.2018.09.018openalex-snapshot
Reduction of acrylamide formation in fried potato chips by Aureobasidum pullulans L1 strain
inferred← citeshttps://doi.org/10.1016/j.jbiosc.2018.09.007openalex-snapshot
Gene cloning and expression of the l-asparaginase from Bacillus cereus BDRD-ST26 in Bacillus subtilis WB600
inferred← citeshttps://doi.org/10.1016/j.jbiosc.2019.06.001openalex-snapshot
Improvement of the activity of l-asparaginase I improvement of the catalytic activity of l-asparaginase I from Bacillus megaterium H-1 by in vitro directed evolution
inferred← citeshttps://doi.org/10.1016/j.jbiosc.2020.01.007openalex-snapshot
Characterization of a novel type I l-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips
inferred← citeshttps://doi.org/10.1016/j.jcs.2013.11.002openalex-snapshot
Reducing the potential for processing contaminant formation in cereal products
inferred← citeshttps://doi.org/10.1016/j.jcs.2022.103485openalex-snapshot
Mitigation of acrylamide formation during malt processing
inferred← citeshttps://doi.org/10.1016/j.jfca.2015.03.009openalex-snapshot
Carcinogenic and neurotoxic risks of acrylamide and heavy metals from potato and corn chips consumed by the Lebanese population
inferred← citeshttps://doi.org/10.1016/j.lwt.2011.02.004openalex-snapshot
Acrylamide reduction in potato chips by using commercial asparaginase in combination with conventional blanching
inferred← citeshttps://doi.org/10.1016/j.lwt.2016.04.017openalex-snapshot
Acrylamide mitigation in French fries using native l-asparaginase from Aspergillus oryzae CCT 3940
inferred← citeshttps://doi.org/10.1016/j.lwt.2017.09.048openalex-snapshot
Evaluation of acrylamide reduction potential of l-asparaginase from Fusarium culmorum (ASP-87) in starchy products
inferred← citeshttps://doi.org/10.1016/j.lwt.2019.04.050openalex-snapshot
Purification and characterization of thermostable l-asparaginase from Bacillus amyloliquefaciens MKSE in Korean soybean paste
inferred← citeshttps://doi.org/10.1016/j.lwt.2024.116365openalex-snapshot
Asparaginase treatment to mitigate acrylamide formation in wheat and rye cookies
inferred← citeshttps://doi.org/10.1016/j.lwt.2024.116770openalex-snapshot
Reducing the acrylamide concentration in homemade bread processed with L-asparaginase
inferred← citeshttps://doi.org/10.1016/j.lwt.2025.118304openalex-snapshot
Refining L-asparaginase application for acrylamide reduction in sweet potatoes
inferred← citeshttps://doi.org/10.1016/j.molcatb.2014.08.021openalex-snapshot
Biochemical characterization of an extremely thermostable l-asparaginase from Thermococcus gammatolerans EJ3
inferred← citeshttps://doi.org/10.1016/j.molcatb.2015.12.007openalex-snapshot
Partial purification and characterization of L-asparaginase from an endophytic Talaromyces pinophilus isolated from the rhizomes of Curcuma amada
inferred← citeshttps://doi.org/10.1016/j.molcatb.2016.06.011openalex-snapshot
Cloning, expression and characterization of aeruginosa EGYII L-Asparaginase from Pseudomonas aeruginosa strain EGYII DSM 101801 in E.coli BL21(DE3) pLysS
inferred← citeshttps://doi.org/10.1016/j.procbio.2018.05.002openalex-snapshot
Improvement of l -asparaginase thermal stability by regulating enzyme kinetic and thermodynamic states
inferred← citeshttps://doi.org/10.1016/j.psep.2024.12.118openalex-snapshot
Bioprospecting of microbial L-asparaginase: Sustainable production from waste and its application for acrylamide reduction in food industry
inferred← citeshttps://doi.org/10.1016/j.sciaf.2023.e01698openalex-snapshot
Acrylamide reduction in potato chips as functional food product via application of enzymes, baker's yeast, and green tea powder
inferred← citeshttps://doi.org/10.1016/j.toxrep.2024.101751openalex-snapshot
Strategies to reduce neurotoxic acrylamide in biscuits, a systematic review
inferred← citeshttps://doi.org/10.1021/acs.jafc.4c06175openalex-snapshot
Influence of Asparaginase on Acrylamide Content, Color, and Texture in Oat, Corn, and Rice Cookies
inferred← citeshttps://doi.org/10.1021/acsfoodscitech.4c00801openalex-snapshot
Acrylamide in Food: Bibliometric Analysis, Chemical-Biological Mitigation, and Future Research Directions
inferred← citeshttps://doi.org/10.1021/acsomega.2c01127openalex-snapshot
Insights into the Distribution and Functional Properties of l ‑Asparaginase in the Archaeal Domain and Characterization of Picrophilus torridus Asparaginase Belonging to the Novel Family Asp2like1
inferred← citeshttps://doi.org/10.1021/acsomega.7b01429openalex-snapshot
Agro Waste Utilization for Cost-Effective Production of l -Asparaginase by Pseudomonas plecoglossicida RS1 with Anticancer and Acrylamide Mitigation Potential
inferred← citeshttps://doi.org/10.1021/jf1042486openalex-snapshot
Implementation of Acrylamide Mitigation Strategies on Industrial Production of French Fries: Challenges and Pitfalls
inferred← citeshttps://doi.org/10.1021/jf305085ropenalex-snapshot
Industrially Applicable Strategies for Mitigating Acrylamide, Furan, and 5-Hydroxymethylfurfural in Food
inferred← citeshttps://doi.org/10.1038/s41598-018-26241-7openalex-snapshot
Simultaneous cell disruption and semi-quantitative activity assays for high-throughput screening of thermostable L-asparaginases
inferred← citeshttps://doi.org/10.1039/9781788016438-00045openalex-snapshot
Risk/Benefits Evaluation of Acrylamide Mitigation Initiatives in Cereal Products
inferred← citeshttps://doi.org/10.1039/c5fo00320bopenalex-snapshot
Acrylamide: inhibition of formation in processed food and mitigation of toxicity in cells, animals, and humans
inferred← citeshttps://doi.org/10.1039/c5fo00655dopenalex-snapshot
Acrylamide mitigation strategies: critical appraisal of the FoodDrinkEurope toolbox
inferred← citeshttps://doi.org/10.1039/c5fo01294eopenalex-snapshot
A review of the interactions between acrylamide, microorganisms and food components
inferred← citeshttps://doi.org/10.1063/5.0195657openalex-snapshot
Acrylaway® L activity on model asparagine to inhibit acrylamide and 5-hydroxymethylfurfural (HMF) formation in Malaysian curry puff skin
inferred← citeshttps://doi.org/10.1080/07388551.2026.2669312openalex-snapshot
Therapeutic recombinant L-asparaginases: a comprehensive review and way forward
inferred← citeshttps://doi.org/10.1080/10242422.2021.2018420openalex-snapshot
Sequential optimization of bioprocess nutritional parameters for maximum l -asparaginase production from Pseudomonas aeruginosa BGR1I1
inferred← citeshttps://doi.org/10.1080/10408398.2019.1588222openalex-snapshot
Acrylamide in human diet, its metabolism, toxicity, inactivation and the associated European Union legal regulations in food industry
inferred← citeshttps://doi.org/10.1080/10826068.2016.1201683openalex-snapshot
Optimization of L -asparaginase production from novelEnterobactersp., by submerged fermentation using response surface methodology
inferred← citeshttps://doi.org/10.1080/10826068.2019.1566152openalex-snapshot
Extracellular L-asparaginase production in solid-state fermentation by using sugarcane bagasse as support material
inferred← citeshttps://doi.org/10.1080/10826068.2025.2559284openalex-snapshot
Characterization of a novel Glutaminase-free L- asparaginase from Bifidobacterium thermophilum
inferred← citeshttps://doi.org/10.1080/19440049.2012.690349openalex-snapshot
Acrylamide formation and antioxidant level in biscuits related to recipe and baking
inferred← citeshttps://doi.org/10.1080/19440049.2024.2379388openalex-snapshot
Trends in acrylamide content in selected potato/sweet potato products on the Canadian market
inferred← citeshttps://doi.org/10.1080/87559129.2021.2023171openalex-snapshot
Mitigation Strategies to Reduce Acrylamide in Cookies: Effect of Formulation
inferred← citeshttps://doi.org/10.1080/87559129.2023.2164896openalex-snapshot
Strategies to Reduce Acrylamide Formation During Food Processing Focusing on Cereals, Children and Toddler Consumption: A Review
inferred← citeshttps://doi.org/10.1088/1742-6596/1341/3/032018openalex-snapshot
Purification, characterization and anticancer potential tests of L-asparaginase enzyme from the leaves siam weed (Chromolaena odorata Linn)
inferred← citeshttps://doi.org/10.1108/nfs-09-2020-0341openalex-snapshot
Is Acrylamide really a food safety issue?
inferred← citeshttps://doi.org/10.1111/1750-3841.70081openalex-snapshot
Evaluation of the effect of enzymatic pretreatment with l ‐asparaginase on acrylamide formation during microwave, air, and deep frying of potatoes
inferred← citeshttps://doi.org/10.1111/febs.16042openalex-snapshot
Structural and biochemical properties of L‐asparaginase
inferred← citeshttps://doi.org/10.1111/j.1750-3841.2012.02664.xopenalex-snapshot
Effect of Radio Frequency Postdrying of Partially Baked Cookies on Acrylamide Content, Texture, and Color of the Final Product
inferred← citeshttps://doi.org/10.1111/jfbc.12756openalex-snapshot
Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules
inferred← citeshttps://doi.org/10.1128/aem.03523-13openalex-snapshot
Biochemical Characterization of a Novel l -Asparaginase with Low Glutaminase Activity from Rhizomucor miehei and Its Application in Food Safety and Leukemia Treatment
inferred← citeshttps://doi.org/10.1134/s0003683823602937openalex-snapshot
A Comprehensive Review of L-Asparaginase: Production, Applications and Therapeutic Potential in Cancer Treatment
inferred← citeshttps://doi.org/10.1134/s0026261724609680openalex-snapshot
Comparative Activity of L-Asparaginases from Thermophiles Thermococcus sibiricus and Melioribacter roseus in Acrylamide Reduction
inferred← citeshttps://doi.org/10.1146/annurev-food-022811-101114openalex-snapshot
Acrylamide in Foods: A Review of the Science and Future Considerations
inferred← citeshttps://doi.org/10.1155/2015/627031openalex-snapshot
Optimization of Culture Conditions for Production of the Anti-Leukemic Glutaminase Free L-Asparaginase by Newly IsolatedStreptomyces olivaceusNEAE-119 Using Response Surface Methodology
inferred← citeshttps://doi.org/10.11606/d.97.2016.tde-25022016-093904openalex-snapshot
Aspectos da produção de L-asparaginase por leveduras
inferred← citeshttps://doi.org/10.11606/d.97.2017.tde-30062017-200104openalex-snapshot
Produção de L-asparaginase extracelular por fermentação em estado sólido
inferred← citeshttps://doi.org/10.1201/9781315371443-22openalex-snapshot
Industrial Food Processing Contaminants
inferred← citeshttps://doi.org/10.1201/b19408-3openalex-snapshot
Enzymes: Concepts, Nomenclature, Mechanism of Action and Kinetics, Characteristics and Sources of Food-Grade Enzymes
inferred← citeshttps://doi.org/10.1201/b19408-7openalex-snapshot
Enzymes: Concepts, Nomenclature, Mechanism of Action and Kinetics, Characteristics and Sources of Food-Grade Enzymes
inferred← citeshttps://doi.org/10.14419/ijet.v7i3.34.18980openalex-snapshot
Classification and Privacy Preserving Search of Multimedia Data
inferred← citeshttps://doi.org/10.14429/dlsj.9.19358openalex-snapshot
Microbial L Asparaginases Therapeutic and Industrial Applications
inferred← citeshttps://doi.org/10.1515/biolog-2016-0168openalex-snapshot
TK1656, an L-asparaginase from Thermococcus kodakarensis, a novel candidate for therapeutic applications
inferred← citeshttps://doi.org/10.1533/9780857095695.2.470openalex-snapshot
Applications of enzymes in breadmaking
inferred← citeshttps://doi.org/10.15414/jmbfs.2019.9.2.179-190openalex-snapshot
L-ASPARAGINASE AND L-GLUTAMINASE: SOURCES, PRODUCTION, AND APPLICATIONS IN MEDICINE AND INDUSTRY
inferred← citeshttps://doi.org/10.18052/www.scipress.com/ilns.15.23openalex-snapshot
L-Asparaginase: An Ultimate Anti-Neoplastic Enzyme
inferred← citeshttps://doi.org/10.20473/jipk.v10i2.10467openalex-snapshot
Identifikasi Bakteri Endofit Mangrove Api-Api Putih (Avicennia marina) Penghasil Enzim L-asparaginase [Identification of Mangrove Endophyte Bacteria of Api-Api Putih (Avicennia marina) as Producing L-asparaginase Enzyme]
inferred← citeshttps://doi.org/10.21203/rs.3.rs-3113826/v1openalex-snapshot
Characterization of a Novel Glutaminase-free L-asparaginase from Bifidobacterium Thermophilum
inferred← citeshttps://doi.org/10.21608/aps.2019.20220openalex-snapshot
Diverse origins of microbial L-asparaginases and their current miscellaneous applications
inferred← citeshttps://doi.org/10.21608/bfszu.2022.138237.1139openalex-snapshot
L-Asparaginase, a promising enzyme in food industry
inferred← citeshttps://doi.org/10.21608/ejah.2023.316048openalex-snapshot
Marine-Derived L-asparaginase as anti-Microbial and Food Preservative against Listeria monocytogenes isolated from Basa Fish Fillet (Pangasius bocourti)
inferred← citeshttps://doi.org/10.2174/1389203720666181114111035openalex-snapshot
Insights into the Microbial L-Asparaginases: from Production to Practical Applications
inferred← citeshttps://doi.org/10.2174/2211550109666200206100445openalex-snapshot
Bioprocess Optimization for Enhanced Production of L-asparaginase via Two Model-Based Experimental Designs by Alkaliphilic Streptomyces fradiae NEAE-82
inferred← citeshttps://doi.org/10.21931/rb/2022.07.01.28openalex-snapshot
Purification and characterization of L-asparaginase extracted from local Iraqi green beans (Phaseoulus vulgaris)
inferred← citeshttps://doi.org/10.22159/ajpcr.2018.v11i10.27073openalex-snapshot
ACRYLAMIDE: A POSSIBLE RISK FACTOR FOR CARDIAC HEALTH
inferred← citeshttps://doi.org/10.2217/fmb-2023-0131openalex-snapshot
Heterologous Expression of Fungal L-Asparaginase: A Systematic Review
inferred← citeshttps://doi.org/10.22587/ajbas.2018.12.11.18openalex-snapshot
Production of Antileukemic Enzyme L-asparaginase from Marine Bacteria Associated with Coral Siderastrea stellate (Verrill, 1868), Brazil
inferred← citeshttps://doi.org/10.2478/s11756-018-0054-1openalex-snapshot
Gene cloning and characterization of recombinant L-Asparaginase from Bacillus subtilis strain R5
inferred← citeshttps://doi.org/10.25439/rmt.27332688openalex-snapshot
Studies of niacin and acrylamide during processing of instant Asian noodles
inferred← citeshttps://doi.org/10.2903/j.efsa.2015.4104openalex-snapshot
Scientific Opinion on acrylamide in food
inferred← citeshttps://doi.org/10.3109/1040841x.2015.1022505openalex-snapshot
A critical review on properties and applications of microbial l -asparaginases
inferred← citeshttps://doi.org/10.33448/rsd-v10i10.18980openalex-snapshot
L-asparaginase: therapeutic use and applications in the food industry – a review
inferred← citeshttps://doi.org/10.3389/fmicb.2021.641251openalex-snapshot
Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure–Function Relationship and Its Biotechnological Applications
inferred← citeshttps://doi.org/10.3390/agronomy9110713openalex-snapshot
Impact of Row Distance and Seed Density on Grain Yield, Quality Traits, and Free Asparagine of Organically Grown Wheat
inferred← citeshttps://doi.org/10.3390/app11093943openalex-snapshot
Characteristics of French Fries and Potato Chips in Aspect of Acrylamide Content—Methods of Reducing the Toxic Compound Content in Ready Potato Snacks
inferred← citeshttps://doi.org/10.3390/app15073779openalex-snapshot
Effect of Asparaginase Treatment on Biscuit Volatile Compounds
inferred← citeshttps://doi.org/10.3390/app16136750openalex-snapshot
Effect of Asparaginase on Neo-Formed Contaminants and Quality Attributes in Wholemeal Biscuits
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