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

Abstract

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.

Potential of Low Cost Agro-Industrial Wastes as a Natural Antioxidant on Carcinogenic Acrylamide Formation in Potato Fried Chips

“…The pre-processing method before frying such as blanching, addition of salts, soaking, addition of vinegar, organic acids, and antioxidants has also been discovered for acrylamide mitigation. Use of enzymes, such asparaginase, to prevent the formation of acrylamide through the enzymatic conversion of L-asparagine to ammonia and L-aspartic acid has also been observed as a mitigation technique [ 10 ]. However, even when produced from diffused and renewable sources, the price of enzymes remains expensive [ 11 ].…”

Substrate Affinity Is Not Crucial for Therapeutic L-Asparaginases: Antileukemic Activity of Novel Bacterial Enzymes

“…However, this information is not supported by sequence databases, as the B. licheniformis genome does not encode an L-asparaginase with such a high M w . It was also shown that an enzyme isolated from soybean root nodules (K m for L-Asn 0.36 mM) had higher antiproliferative activity in MOLT-4 and HL-60 cells than EcAII [56]. It is possible that the extracted protein was a thermolabile class 3 L-asparaginase.…”

Overview of the structure, side effects, and activity assays of l-asparaginase as a therapy drug of acute lymphoblastic leukemia

“…response induced by the higher glutaminase activity of the EcA drug, such as the screening of L-ASNase from bacteria, fungi, and yeast, for high throughput. 18,[67][68][69][70][71][72] At the same time, researchers are not only exploring possible sources of production, but also experimenting with different immobilization methods to enhance therapeutic efficacy, such as the novel p(HEMA-GMA) cryogel invented by Noma et al which resulted in a significant increase in enzyme activity and stability, and Ca-ALG/MWCNT-COOH hybrid beads designed by Ulu et al which enhanced the affinity of the enzyme for the substrate. [73][74][75] 4.…”