Degradation Of Acrylamide Research Articles

Theoretical studies on the aqueous phase and graphene heterogeneous degradation of acrylamide and acrylonitrile by HO, ClO, and BrO radicals

The newly discovered ClO• and BrO• contribute to pollutant degradation in advanced oxidation processes, while acrylamide (AM) and acrylonitrile (ACN) are always the focus of scientists concerned due to their continuous production and highly toxic effects. Moreover, various particles with a graphene-like structure are the companions of AM/ACN in dry/wet sedimentation or aqueous phase existence, which play an important role in heterogeneous oxidation. Thus, this work focuses on the reaction mechanism and environmental effect of AM/ACN with ClO•/BrO•/HO• in the water environment under the influence of graphene (GP). The results show that although the reactivity sequence of AM and ACN takes the order of with HO• > with BrO• > with ClO•, the easiest channel always occurs at the same C-position of the two reactants. The reaction rate constants (k) of AM with three radicals are 2 times larger than that with ACN, and amide groups have a better ability to activate CC bonds than cyanide groups. The existence of GP can accelerate the target reaction, and the k increased by 9–13 orders of magnitude. The toxicity assessment results show that the toxic effect of most products is lower than that of parent compounds, but the environmental risk of products from ClO•/BrO•-adducts is higher than those from HO•-adducts. The oxidative degradation process based on ClO• and BrO• deserves special attention, and the catalytic effect of GP and its derivatives on the oxidation process is non-negligible.

Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.

The L-asparaginase (ASPN) enzyme has received recognition in various applications including acrylamide degradation in the food industry. The synthesis and application of thermostable ASPN enzymes is required for its use in the food sector, where thermostable enzymes can withstand high temperatures. To achieve this goal, the bacterium Bacillus subtilis was isolated from the hot springs of Tapovan for screening the production of thermostable ASPN enzyme. Thus, ASPN with a maximal specific enzymatic activity of 0.896 U/mg and a molecular weight of 66kDa was produced from the isolated bacteria. The kinetic study of the enzyme yielded a Km value of 1.579mM and a Vmax of 5.009µM/min with thermostability up to 100min at 75°C. This may have had a positive indication for employing the enzyme to stop polyacrylamide from being produced. The current study has also been extended to investigate the interaction of native and mutated ASPN enzymes with acrylamide. This concluded that the M10 (with 10 mutations) has the highest protein and thermal stability compared to the wild-type ASPN protein sequence. Therefore, in comparison to a normal ASPN and all other mutant ASPNs, M10 is the most favorable mutation. This research has also demonstrated the usage of ASPN in food industrial applications.

Production, characterization, and applications of a novel thermo-acidophilic L-asparaginase of Pseudomonas aeruginosa CSPS4

In present investigation, a potential L-asparaginase-producing bacterial isolate, Pseudomonas aeruginosa CSPS4, has been explored to enhance the production and purification of the asparaginase enzyme. Production of L-asparaginase is enhanced using the 'one variable at a time approach (OVAT)'. In Placket Burman (PB) analysis, pH, sucrose, and temperature significantly influence L-asparaginase production. Thereafter, L-asparaginase enzyme was recovered from culture broth using fractional precipitation with chilled acetone. The partially purified L-asparaginase showed a molecular weight of ~35 KDa on SDS-PAGE. L-asparaginase was characterized as a thermo-acidophilic enzyme exhibiting optimum pH and temperature of 6.0 and 60 °C, respectively. These characteristics render this enzyme novel from other available asparaginases of Pseudomonas spp. L-asparaginase activity remained unaffected by different modulators. L-asparaginase of this investigation was successfully employed for acrylamide degradation in commercial fried potato chips, establishing its applicability in food industries.

Biochemical Characterization of Thermostable Acrylamide Amidohydrolase from Aspergillus fumigatus with Potential Activity for Acrylamide Degradation in Various Food Products

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.

Iron/carbon conductive materials for enhancing anaerobic treatment of synthetic acrylamide wastewater

AbstractBACKGROUNDMost studies have focused on the degradation of acrylamide (AM) by a single strain. There are relatively few studies on the treatment of AM by anaerobic activated sludge. Previous studies have shown that conductive particles can change the mode of electron transport between anaerobic microorganisms. Therefore, this study compared the enhancement effect of three different particles (Fe3O4, granular activated carbon (GAC), graphite) on the treatment of synthetic AM wastewater by anaerobic activated sludge under different temperature conditions (30, 25, 20 °C) and particle dose (2, 6 g L−1).RESULTSThe results showed that 6 g L−1 GAC improved the removal rate of chemical oxygen demand (COD) and AM by 22.95% and 19% compared with the control group at 30 °C, respectively, indicating that the addition of GAC contributes to the degradation of AM and improves COD removal rate. Results of high‐performance liquid chromatography (HPLC) showed that the activated sludge with GAC obviously promoted the degradation of AM. Besides, a large amount of propionic acid was detected in all experimental groups during the reaction, and the activated sludge with GAC promoted degradation of propionic acid.CONCLUSIONAnaerobic activated sludge supplemented with sufficient GAC can not only absorb and degrade AM synchronously but also accelerate the conversion of intermediates, such as acrylic and propionic acids. Based on the results of HPLC and liquid chromatography–mass spectrometry, a possible method of degradation of AM by anaerobic activated sludge was proposed. © 2023 Society of Chemical Industry (SCI).

The Acrylamide Degradation by Probiotic Strain Lactobacillus acidophilus LA-5.

Acrylamide is a harmful substance produced in thermal processed food; however, it can also be found in food with various additives. The aim of the study was to check whether the probiotic bacteria strain, Lactobacillus acidophilus LA-5 (LA5), can degrade acrylamide and hence reduce its concentration in foodstuff. Our results revealed that LA5 can degrade acrylamide and cause a decrease in its concentration, but only when other available carbon and nitrogen sources are lacking. In the presence of casein, lactose, milk fat or in whole cow’s milk, this ability disappeared. Acrylamide present in milk, however, modulated the bacteria metabolism by significantly enhancing lactic acid production by LA5 in milk (at conc. 100 µg/mL), while the production of acetic acid was rather reduced.

The Utilisation of Acrylamide by Selected Microorganisms Used for Fermentation of Food.

Acrylamide (AA) present in food is considered a harmful compound for humans, but it exerts an impact on microorganisms too. The aim of this study was to evaluate the impact of acrylamide (at conc. 0–10 µg/mL) on the growth of bacteria (Leuconostoc mesenteroides, Lactobacillus acidophilus LA-5) and yeasts (Saccharomyces cerevisiae, Kluyveromyces lactis var. lactis), which are used for food fermentation. Moreover, we decided to verify whether these microorganisms could utilise acrylamide as a nutritional compound. Our results proved that acrylamide can stimulate the growth of L. acidophilus and K. lactis. We have, to the best of our knowledge, reported for the first time that the probiotic strain of bacteria L. acidophilus LA-5 is able to utilise acrylamide as a source of carbon and nitrogen if they lack them in the environment. This is probably due to acrylamide degradation by amidases. The conducted response surface methodology indicated that pH as well as incubation time and temperature significantly influenced the amount of ammonia released from acrylamide by the bacteria. In conclusion, our studies suggest that some strains of bacteria present in milk fermented products can exert additional beneficial impact by diminishing the acrylamide concentration and hence helping to prevent against its harmful impact on the human body and other members of intestinal microbiota.

Versatile and Valuable Utilization of Amidohydrolase L-glutaminase in Pharma and Food industries: A Review.

L-glutaminase has versatile applications in pharma and food industries. In pharmaceutical industry, L-glutaminase can be used as anti-oxidant and anti-cancer agent to treat Acute Lymphocytic Leukaemia (ALL). Whereas, in the food industry, L-glutaminase is used for acrylamide degradation, theanine production, flavour enhancer, soy sauce and many. The other applications include nitrogen metabolism and its use as biosensor in hybridoma technology. Both intra-cellular and extra-cellular L-glutaminases from wide range of sources were identified. Because of its diverse applications, there is a need to improve the production of L-glutaminase by enzyme engineering technology. Effect of recombination on L-glutaminase production was also reported. Researchers also confirmed the antitumor properties of L-glutaminase by conducting in vitro, in vivo and in silico studies. Bacillus sps. and Aspergillus sps. are the commercial producers of L-glutaminase. In this review, the applications, different sources of Lglutaminase, anti-cancer properties were discussed.

Temperature Dependence of the Processes of Acrylamide Biodegradation in River Silt Suspensions at Their Inoculation by Selected Bacterial Strains

The temperature dependence of the rate of acrylamide biodegradation by silt microorganisms of small rivers in the Perm krai is studied in the antropogenically polluted Danilikha River, flowing in the territory of Perm city, and the Syuz’va River’s relatively clear tributary in Nytvenskii district. The rate of acrylamide biodegradation increases after introducing into river silt the biomass of bacteria of strains Alcaligenes faecalis 2 and Acinetobacter guillouiae 11h, selected toward an increase in amidase activity. It is shown that, at the ambient temperature of 30°C, the complete degradation of 100 mM acrylamide solution by silt microbiocenosis from the Danilikha River and a tributary of the Syuz’va River has taken place by the 21st and 28th day, respectively, while at 5 and 16–20°C, acrylamide concentration has decreased only slightly even by the 63rd day. The introduction of the biomass of preselected bacteria considerably reduces the time required for complete degradation of acrylamide. At temperature 5°C, acrylamide utilization can take place only at inoculation of silts by the biomass of amidase-containing microorganisms. A mathematical model of acrylamide biodegradation in silt suspensions of small rivers is given; kinetic curves of changes in its concentration are presented, and temperature dependences of biodegradation rates are obtained for different variants of the process.

Cross-linked enzyme aggregates of arylamidase from Cupriavidus oxalaticus ICTDB921: process optimization, characterization, and application for mitigation of acrylamide in industrial wastewater.

Acrylamidase produced by Cupriavidus oxalaticus ICTDB921 was recovered directly from the fermentation broth by ammonium sulfate (40-50%) precipitation and then stabilized by cross-linking with glutaraldehyde. The optimum conditions for the preparation of cross-linked enzyme aggregates of acrylamidase (acrylamidase-CLEAs) were using 60mM glutaraldehyde for 10min at 35°C and initial broth pH of 7.0. Acrylamidase-CLEAs were characterized by SDS-PAGE, FTIR, particle size analyzer and SEM. Cross-linking shifted the optimal temperature and pH from 70 to 50°C and 5-7 to 6-8, respectively. It also altered the secondary structure fractions, pH and thermal stability along with the kinetic constants, Km and Vmax, respectively. A complete degradation of acrylamide ~ 1.75g/L in industrial wastewater was achieved after 60min in a batch process under optimum operating conditions, and the kinetics was best represented by Edward model (R2 = 0.70). Acrylamidase-CLEAs retained ~ 40% of its initial activity after three cycles for both pure acrylamide and industrial wastewater, and were stable for 15days at 4°C, retaining ~ 25% of its original activity.

Acrylamide determination during an industrial roasting process of coffee and the influence of asparagine and low molecular weight sugars

The formation and partial degradation of acrylamide (AA), asparagine and low molecular weight sugars were evaluated during an industrial coffee roasting process, in which the temperature increased from 90° to about 215 °C. Arabica and Robusta varieties were roasted individually. AA content reached the maximum value at 10 min, corresponding to a temperature of 175–177 °C (1045 ± 28 and 795 ± 25 µg kg−1 for Arabica and Robusta, respectively). Successively, AA content decreased very quickly and at 14 min (203–205 °C) its concentration was lower than the benchmark level of 400 µg kg−1 for roast coffee set by the EU Commission Regulation (2017/2158). In the final product, AA content was close to 300 µg kg−1. Asparagine quickly decreased; contrary, the concentration of fructose and glucose increased reaching their maximum value at 12 min. Then, a quick degradation occurred; their increase could be mainly due to the hydrolysis of sucrose, which decreased in the same period.

Screening, optimization of culture conditions and scale-up for production of the L-Glutaminase by novel isolated Bacillus sps. mutant endophyte using response surface methodology

Abstract L-Glutaminase is known as the anti-cancer drug to treat anti-leukemic cancer besides its use in food industry for the acrylamide degradation of fried foods. In the present study, submerged fermentation was carried out for the production; statistical based experimental designs were employed to optimize the culture conditions and to maximize the L -Glutaminase activity from novel Bacillus sps., mutant endophyte isolated from Ocimum tenuiflorum. Eleven process variables of the medium were examined for their significance using Plackett-Burman design on the production of L-Glutaminase i.e., Galactose, L -Glutamine, Na2HPO4, KH2PO4, NaCl, MgSO4·H2O, Yeast extract, pH, Temperature, RPM, Time were screened and it was observed that activity was 22.49 IU/ml. After Plackett-Burman design experiments, the activity was found to be 2.34 folds increase compared to one variable at a time method. Further, the production was optimized with Response Surface Methodology (RSM) using Central Composite Design (CCD) for significant variables i.e., Galactose (g/L), Time (h), Temperature (T°C) and pH obtained from Plackett-Burman design and the activity was found to be 24.585 IU/ml i.e., 2.56 fold increment in the production compared to unoptimized medium. Experimentation revealed that the isolated novel Bacillus sps., mutants as the potential bacterial source for L -Glutaminase production.

Characterisation of an Acrylamide-Degrading Bacterium and Its Degradation Pathway

Widespread use of acrylamide by the industry led to the environmental pollution that results from the indiscriminate discharge of acrylamide. The presence of acrylamide in the environment is a major threat due to its neurotoxic, carcinogenic and teratogenic properties. In this work bacterial isolate identified as Burkholderia sp. strain AQ5-13 is capable of degrading acrylamide as both its carbon and nitrogen sources were screen based on the capability of the bacteria to grow on solid basal salt media that contain 500 mg/L acrylamide as sole carbon and nitrogen sources without supplementation of additional carbon or nitrogen sources. Bacteria grow curve study was carried out by measuring the absorbance value at 600 nm. Burkholderia sp. strain AQ5-13 showed a complete life cycle in five days of incubation with no lag phase identified at the earlier growth phase. Optimum conditions for acrylamide degradation was conducted at different initial pH and incubation temperature. Growth optimisation of the bacteria was measured by plate counting in CFU after 48 h of incubation in 250 mL basal salt media that contain 500 mg/L acrylamide. Burkholderia sp. strain AQ5-13 showed optimum growth in acidic media at pH 5.7 (5.57 log 10 CFU/mL) and optimum growth at 30°C (6.84 log 10 CFU/mL) compared to other temperature ranges. Quantitative monitoring of acrylamide degradation was performed using HPLC. Burkholderia sp. strain AQ5-13 could degrade 14% of 500 mg/L acrylamide as its carbon and nitrogen sources after 72 h of incubation at 5 min of retention time. The appearance of acrylic acid peak as an intermediate was not detected, possibly because all the acrylic acid produced had been consumed immediately by the bacterium. The result from this study showed that bacteria Burkholderia sp. strain AQ5-13 has a good potential that can be applied in the bioremediation of waste containing acrylamide.

Magnetic cross-linked enzyme aggregates of acrylamidase from Cupriavidus oxalaticus ICTDB921 for biodegradation of acrylamide from industrial waste water

Acrylamidase from Cupriavidus oxalaticus ICTDB921 was immobilized on magnetic nanoparticles (MNPs) for degradation of acrylamide (a group 2A carcinogen and an environmental contaminant) from industrial waste water. Acrylamidase-MNPs were prepared (maximum recovery ∼94%) at optimized process parameters viz. 1.5:1 (v/v) of acetone: crude acrylamidase/5 mM of glutaraldehyde/90 min/1.5:1 of enzyme: MNP ratio. MNPs and acrylamidase-MNPs were characterized by particle size analysis, FTIR, XRD, SEM and vibrating sample magnetometer. Acrylamidase-MNPs showed a shift in optimum pH (8–8.5) and temperature (60–65 °C) with higher pH/thermal stability vis-à-vis free enzyme. A significant increase in kinetic constants, thermal inactivation constants and thermodynamic parameters were noted for acrylamidase-MNPs. A complete degradation of acrylamide ∼2100 mg/L was achieved in industrial waste water under optimized conditions for batch process and the kinetics was best represented by Haldane model. Acrylamidase-MNPs retained >80% of its initial activity after 4 cycles for both pure acrylamide and industrial waste water.

Biodegradation of acrylamide by a novel isolate, Cupriavidus oxalaticus ICTDB921: Identification and characterization of the acrylamidase produced

Acrylamide is neurotoxic, genotoxic, teratogenic and carcinogenic. Its widespread use in various industrial processes leads to environmental contamination. Acrylamidase produced by certain bacteria degrade acrylamide to acrylic acid and ammonia. The present study details the isolation and identification of soil bacterium which could degrade acrylamide. Among the 18 acrylamide-degrading isolates tested, isolate ICTDB921 demonstrated superior acrylamide degradation which was confirmed by HPLC, FTIR and GC-MS. The partial 16S rRNA sequencing confirmed the isolate to be Cupriavidus oxalaticus ICTDB921, which showed highest growth at 60 mM acrylamide, neutral pH and 30 °C. The kinetic model predictions were consistent with experimental results. The acrylamidase from this isolate showed potency at pH (6–8) and temperatures (30–60 °C), with reasonable pH (6–8) and thermal stability (upto 60 °C). The enzyme was stable against most metal ions and amino acids, and also degraded other aliphatic amides, demonstrating its potential in remediation of acrylamide from the environment and food systems.

Acrylamide in Environmental Water: A Review on Sources, Exposure, and Public Health Risks

Acrylamide and polyacrylamide (PAM) are used in diverse industrial processes, mainly the production of plastics, dyes, and paper, in the treatment of drinking water, wastewater, and sewage. Besides inorganic form, acrylamide is formed naturally in certain starchy foods that were heated to cook a temperature above 120 °C for elongated time. Researches in rats have demonstrated that acrylamide exposure poses a risk as a neurotoxin to humans and also classified as a carcinogenic and mutagenic compound. Acrylamide may be released into drinking water supplies from its wide-ranging industrial use. Acrylamide has high risk of contamination into surface and ground water supplies due to its rapid solubility and mobility in water. Bacterial use of acrylamide as nitrogen and carbon source is the main pathway of its degradation in water. The degradation of acrylamide in water occurs about 8–12 days depending on water conditions. International Agency for Research on Cancer has declared acrylamide as 2A Group carcinogen in 1994. The major concern related to acrylamide contamination is arising from organic source that occurs especially by consumption of heated starchy food. On the other hand, as acrylamide or PAM is commonly used in different industrial processes, inorganic acrylamide contamination into environment is a big threat and has potential hazards for public health. The main objective of the present review is to summarize the routes of acrylamide contamination, degradation, release and transfer into environmental water, as well as to present integrated information on acrylamide chemistry, toxicity, and analyses, together with potential safety risks for public health. Recommended actions and further studies in needed areas are suggested.

Degradation of acrylamide during chlorination as a precursor of haloacetonitriles and haloacetamides

Acrylamide is a monomer of polyacrylamide, which is widely used in the water treatment process as a flocculant. The degradation kinetics and formation of disinfection by-products (DBPs) during acrylamide chlorination were investigated in this study. The reaction between chlorine and acrylamide followed a pseudo-first-order kinetics. A kinetic model regarding acrylamide chlorination was established and the rate constants of each predominant elementary reaction (i.e., the base-catalyzed reaction of acrylamide with ClO− as well as the reactions of acrylamide with HOCl and ClO−) were calculated as 7.89×107M−2h−1, 7.72×101M−1h−1, and 1.65×103M−1h−1, respectively. The presence of Br− in water led to the formation of HOBr and accelerated the rate of acrylamide degradation by chlorine. The reaction rate constant of acrylamide with HOBr was calculated as 1.33×103M−1h−1. The degradation pathways of acrylamide chlorination were proposed according to the intermediates identified using ultra-performance liquid chromatography and electrospray ionization-quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF/MS). Five chlorinated DBPs including chloroform (CF), dichloroacetonitrile (DCAN), trichloroacetonitrile (TCAN), dichloroacetamide (DCAcAm), and trichloroacetamide (TCAcAm) were identified during acrylamide chlorination. The formation of CF, DCAN, DCAcAm, and TCAcAm kept increasing, while that of TCAN increased and then decreased with increasing reaction time. As the chlorine dosage increased from 0.75 to 4.5mM, DCAN became the dominant DBP. Large amounts of CF, DCAN, and TCAN were formed at basic pHs. The hydrolysis of DCAN and TCAN led to the formation of DCAcAm and TCAcAm, respectively. The results of this study elucidated that acrylamide can be a precursor for the formation of haloacetonitriles (HANs) and haloacetamides (HAcAms) during drinking water treatment.

Degradation of acrylamide by the UV/chlorine advanced oxidation process

The degradation of acrylamide (AA) during UV/chlorine advanced oxidation process (AOP) was investigated in this study. The degradation of AA was negligible during UV irradiation alone. However, AA could be effectively degraded and mineralized during UV/chlorination due to the generation of hydroxyl radicals (OH). The degradation kinetics of AA during UV/chlorination fitted the pseudo-first order kinetics with the rate constant between AA and OH radicals being determined as 2.11 × 109 M−1 s−1. The degradation rate and mineralization of AA during UV/chlorination were significantly promoted at acidic conditions as well as increasing chlorine dosage. The volatile degradation products of AA during UV/chlorination were identified using gas chromatography-mass spectrometry and the degradation pathways were then proposed accordingly. The formation of disinfection by-products (DBPs) in Milli-Q water and tap water during UV/chlorination of AA was also investigated. The DBPs included chloroform, dichloroacetonitrile, trichloroacetonitrile, 2,2-dichloroacetamide and 2,2,2-trichloroacetamide. Furthermore, the variations of AA degradation during UV/chlorination in different real water samples were evaluated.

Identification of proteins differentially accumulated in Enterococcus faecalis under acrylamide exposure

Analysis of bacterial proteomes can be used to obtain large amounts of information about adaptive microbial mechanisms to changing extracellular conditions. In the past, many bacterial species with the ability to degrade acrylamide were isolated. In this study differences in the Enterococcus faecalis proteome upon acrylamide exposure were investigated. We revealed substantial changes in the proteome of bacteria cultured in different environmental conditions. Microorganisms exposed to acrylamide showed higher accumulation of proteins associated with energy metabolism and its regulation. Moreover, several proteins involved in protection of cells from stress conditions were also identified. These biomacromolecules are involved in proper folding of newly synthesized polypeptides like chaperones or participate in mechanisms of DNA repair. In contradiction with previous reports, the presence of amidase was not detected. However, identification of aminopeptidase with activity to hydrolyze amino acid amides can indicate that it can degrade acrylamide to acrylic acid and ammonia instead of amidase. According to identified proteomic profiles, a new mechanism of acrylamide degradation by Enterococcus faecalis is proposed.

Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC.

The use of bacterial l-asparaginase (LA) is one of the alternative approaches for acrylamide reduction in food stuffs as it catalyzes the conversion of l-asparagine to l-aspartic acid and ammonia. In present investigation, purification of extracellular LA from isolate of Bacillus subtilis sp. strain KDPS-1 was carried out by solid state fermentation process. The effects of solid substrates, initial moisture content, moistening agents, temperature, and incubation time on LA production was studied, and the highest asparaginase activity (47 IU/ml) was achieved in the medium having orange peel as substrate. The enzyme was purified to homogeneity by diethylaminoethyl (DEAE) cellulose ion exchange chromatography; with 84.89 % yield and 12.11 fold purity. LA showed stimulant activity against β-mercaptoethanol and was greatly inhibited by Zn2+ and Hg2+ metal ions. Reduction of acrylamide in fried potatoes was detected by high performance liquid chromatography, which showed clear degradation of acrylamide by height and area (%) in the chromatograms of standard sample to that of the test sample. Hydrolysates analysis by high performance thin layer chromatography confirmed the test sample to be LA.