Biochemical characterization of a novel l-asparaginase from Bacillus megaterium H-1 and its application in French fries

Zhang, Sunyan; Xie, Yajuan; Zhang, Chong; Bie, Xiaomei; Zhao, Haizhen; Lu, Fengxia; Lu, Zhaoxin

doi:10.1016/j.foodres.2015.08.031

Cited by 39 publications

(17 citation statements)

References 42 publications

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“…This is because the enzyme reduces more than 88% of the l -asparagine concentration from the initial feedstock. In last years, other works have dealt with this application of l -asparaginase, that can decrease the negative effects of acrylamide containing foods without impair their characteristics 3, 25, 26, 27, 28…”

Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

175

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l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

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Section: L-asparaginase Applicationsmentioning

confidence: 99%

Current applications and different approaches for microbial l-asparaginase production

Cachumba

Antunes

Peres

et al. 2016

Brazilian Journal of Microbiology

175

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“…The specific activity of SrnASNase toward L‐asparagine was 531.37 U/mg (Table ), which is higher than the reported activity of eubacterial L‐asparaginases from H.pylori (31.2 U/mg) (Cappelletti et al, ), B. megaterium H‐1 (44.7 U/mg) (Zhang et al, ), Bacillus subtilis B11‐06 (92.45 U/mg) (Jia et al, ), Er. chrysanthemi 3,937 (118.7 U/mg) (Kotzia & Labrou, ), Aquabacterium sp .…”

Section: Resultsmentioning

confidence: 67%

“…Many enzymes with L-asparaginase activity are quite specific for L-asparagine, but also have a low level of intrinsic L-glutaminase activity that hydrolyzes the amino acid L-glutamine, which is an undesirable effect for the food industry (Husain, Sharma, Kumar, & Malik, 2016;Shrivastava et al, 2016). Hence, it is necessary to search for novel Lasparaginases since drawbacks in the food industry are increasingly reported (Zhang et al, 2015).…”

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confidence: 99%

Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules

2019

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A novel asparaginase (designated srnASNase) has been purified from soybean root nodules and identified by MALDI‐TOF/TOF‐MS. And the enzymatic properties, antitumor activity and the ability to prevent acrylamide formation in fried foods of srnASNase were evaluated. SrnASNase had high specific activity (531.37 U/mg) toward L‐asparagine under optimum conditions (pH 8.0 and 40°C), no activity toward L‐glutamine and D‐glutamine, but trace activity toward D‐asparagine. It was stable in the pH range of 7.0–9.0 and up to 40°C. The Km and Vmax of srnASNase were 0.36 mM and 51.64 mM/min, respectively. Further, in vitro anti‐proliferative activity on human cancer cells assay showed that srnASNase was superior to commercial asparaginase in solution by controlling the tumor cell growth with time. In addition, srnASNase showed more effective acrylamide mitigation than commercial asparaginase in fried foods. These results indicate that srnASNase is a potential candidate for applications in the food processing and pharmaceutical industry. Practical applications L‐asparaginase (L‐asparagine amidohydrolase; EC 3.5.1.1) is an enzyme that catalyzes the hydrolysis of the amide group of the side‐chain of L‐asparagine into aspartic acid and ammonia. It has long been used as a primary component in the treatment of acute lymphoblastic leukemia (All) and other related blood cancers. Apart from its clinical usage, L‐asparaginase has attracted more attention in the food processing industries as a promising acrylamide‐mitigating agent in recent years. This research revealed that soybean root nodules might be good sources of novel asparaginase.

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“…( )) Previous studies have reported that L-asparaginases from different microorganisms had different substrate affinities and probably played different physiological roles. Higher and lower K m values have been reported for different L-asparaginase enzymes [8, 45]. E. coli L-asparaginase showed K m of 3.4 mM which is similar to that of Bacillus PG04 and lower than the K m value of Bacillus PG03.…”

Section: Resultsmentioning

confidence: 72%

Purification, Characterization and Comparison between Two New L-asparaginases from PG03 and PG04

Rahimzadeh¹,

Poodat²,

Javadpour³

et al. 2016

Open Biochem J.

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Background:L-asparaginase has been used as a chemotherapeutic agent in treatment of lymphoblastic leukemia. In the present investigation, Bacillus sp. PG03 and Bacillus sp. PG04 were studied.Methods:L- asparaginases were produced using different culture media and were purified using ion exchange chromatography.Results:Maximum productivity was obtained when asparagine was used as the nitrogen source at pH 7 and 48 h after cultivation. New intracellular L-asparaginases showed an apparent molecular weight of 25 kDa and 30 kDa by SDS-PAGE respectively. These enzymes were active in a wide pH range (3-9) with maximum activity at pH 6 for Bacillus PG03 and pH 7 for Bacillus PG04 L-asparaginase. Bacillus PG03 enzyme was optimally active at 37 ˚C and Bacillus PG04 maximum activity was observed at 40˚C. Kinetic parameters km and Vmax of both enzymes were studied using L-asparagine as the substrate. Thermal inactivation studies of Bacillus PG03 and Bacillus PG04 L-asparaginase exhibited t1/2 of 69.3 min and 34.6 min in 37 ˚C respectively. Also T50 and ∆G of inactivation were measured for both enzymes.Conclusion: The results revealed that both enzymes had appropriate characteristics and thus could be a potential candidate for medical applications.

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Biochemical characterization of a novel l-asparaginase from Bacillus megaterium H-1 and its application in French fries

Cited by 39 publications

References 42 publications

Current applications and different approaches for microbial l-asparaginase production

Current applications and different approaches for microbial l-asparaginase production

Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules

Purification, Characterization and Comparison between Two New L-asparaginases from PG03 and PG04

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