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The enzyme L asparaginase is used in the treatment of leukemia to stop cancer cells from replicating further.

IIT Hyderabad researchers isolate chemotherapeutic enzyme from Antarctic fungi
Health Cancer Research Wednesday, February 20, 2019 - 19:35

After two years of toiling research, scientists from IIT Hyderabad say they have isolated an enzyme from a fungus found in Antarctica, which may hold the key to treating acute lymphoblastic leukemia (ALL), one of the most common forms of leukemia seen in children. “Around 20,000 children are diagnosed with ALL in India,” states Dr Julius Scott, Pediatric Hemato-oncologist and founder of Medhope Organisation which works with children suffering from leukemia, “Of these around 2,500 children are probably diagnosed in Tamil Nadu alone.” With the latest research findings, scientists are hopeful that a more cost-effective drug with lesser side effects can be manufactured to treat ALL.

“L-asparaginase is a chemotherapeutic drug which is used to treat leukemia. The currently available forms of it contain glutaminase and urease compounds which produce severe unpleasant side effects in those who are administered the drug,” explains Professor Devarai Santhosh Kumar, one of the main researchers and Associate professor at the Department of Chemical Engineering at IIT Hyderabad. He further adds that the purpose of their research is not only to make a version of the drug with fewer side effects, but to make one that is more cost effective and thereby more accessible to all.

The enzyme L-asparaginase is used in the treatment of leukemia as it helps to stop cancer cells from replicating further. The currently used forms of the drug are derived from bacteria, and contain in them two substances called urease and glutaminase, which produce severe side effects ranging from flu-like symptoms, nausea and vomiting, allergic reactions, stomach cramps, and even some neurological effects like agitation, hallucinations, or confusion. The enzyme derived from the fungus is free of urease and glutaminase, which in theory mean that there would be no side effects from the same.

“The L-asparaginase enzyme used for chemotherapy is currently derived from commonly found bacteria such as Escherichia coli and Erwinia chrysanthemi. These enzymes are always associated with two other enzymes, glutaminase and urease, both of which cause adverse side effects in patients. The research team looked at psychrophiles as alternate sources of the enzyme. Psychrophiles are organisms that are capable of growth and reproduction in low temperatures in the range of −20 °C to +10 °C, such as those found in Antarctic regions. These organisms have modified life processes that help them adapt to the extreme conditions of living. For example, psychrophiles have ‘anti-freeze’ enzymes that are powerful enough to be able to work at the freezing temperatures of the poles, unlike mesophiles that live in more habitable zones of the earth. The potency of these enzymes makes them promising as powerful drugs for diseases such as cancer,” reads the press release issued by IIT Hyderabad.

Dr Arif Qureshi

Back in 2017, a team of researchers headed by Dr Arif Qureshi from IIT Hyderabad’s department of civil engineering went to Antarctica for four months. They were able to bring back samples of soil, ice, water, which were then screened at the lab in IIT for the presence of L asparaginase. Now, two years later, they have successfully been able to isolate the enzyme from 33 out of 50 samples that they tested.

“Going forward our plan is to make it more commercialised. We will first have to conduct several clinical trials on cancer cells in animals before we can proceed and take up the same for humans,” said Deverai.

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