Abstract
<p>L-asparaginase merupakan enzim yang mengubah L-asparagin menjadi L-aspartat. L-asparagin dapat dimanfaatkan oleh sel kanker leukemia sebagai salah satu sumber nutrisinya. Penambahan L-asparaginase dapat menghambat pertumbuhan sel kanker. Penggunaan L-asparaginase dalam skala industri lebih mengutamakan L-asparaginase yang memiliki aktivitas dan stabilitas optimum di suhu tinggi, karena kecepatan reaksi dalam menghidrolisis L-asparagin tinggi, stabil dari denaturan misalnya detergen dan senyawa organik, dan stabil pada kondisi asam maupun basa. L-asparaginase yang memiliki aktivitas dan stabilitas di suhu tinggi dapat dieksplorasi dari mikroorganisme yang hidup di lingkungan yang bersuhu dan bersalinitas tinggi. Tujuan penelitian ini adalah untuk memperoleh isolat bakteri termohalofilik penghasil enzim L-aparaginase dari sumber air panas Wawolesea dan untuk mengetahui aktivitas enzim L-asparaginase yang dihasilkannya. Bakteri termohalofilik penghasil enzim L-asparaginase diperoleh dengan tahapan: isolasi bakteri pada media NA yang mengandung NaCl 1,5% – 1,6%; seleksi bakteri penghasil L-asparaginase pada media M-9; produksi L-asparaginase dengan prinsip fermentasi pada media produksi serta pengukuran aktivitas dan aktivitas spesifik enzim L-asparaginase. Hasil isolasi menunjukkan adanya 14 isolat bakteri termohalofilik yang mampu menghasilkan enzim L-asparaginase. Aktivitas enzim L-asparaginase tertinggi yaitu 86,61 IU/mL pada isolat AAT3.2 dan terendah yaitu 38,24 IU/mL pada isolat CAT1.1. Aktivitas spesifik tertinggi 6767,98 IU/mg pada isolat CAT3.2 dan terendah 684,54 IU/mg pada isolat CAT1.1.</p><p><strong>Screening of L-asparaginase-Producing Thermohalophilic Bacteria from Wawolesea Hot Springs in Southeast Sulawesi and Their Enzyme Activity Test.</strong> The L-asparaginase is an enzyme that can convert L-asparagine to L-aspartate. L-asparagine can be utilized by leukemia cancer cells as a source of nutrition. The use of L-asparaginase on an industrial scale prioritizes L-asparaginase that exhibits optimal activity and stability at high temperatures due to the high reaction rate in hydrolyzing L-asparagine, stability against denaturants such as detergents and organic compounds, and stability under acidic or basic conditions. L-asparaginase with activity and stability at high temperatures can be explored from microorganisms that live in high-temperature and high-salinity environments.<strong> </strong>This study aimed to obtain isolates of thermohalophilic bacteria that produce L-asparaginase enzymes from Wawolesea hot springs and determine the activity of the L-asparaginase enzymes. Thermohalophilic bacteria producing L-asparaginase from Wawolesea hot springs were obtained by the following steps: isolation of bacteria on NA (Nutrient Agar) media containing 1.5% – 1.6% NaCl, selection of L-asparaginase-producing bacteria on M-9 media, production of L-asparaginase with the principle of fermentation on production media and measurement of activity and specific activity of L-asparaginase enzyme. The isolation results showed that there were 14 isolates of thermohalophilic bacteria capable of producing L-asparaginase. The highest L-asparaginase enzyme activity was 86.61 IU/mL in AAT3.2 isolates, and the lowest was 38.24 IU/mL in CAT1.1 isolates. The highest specific activity was 6767.98 IU/mg in isolate CAT3.2, and the lowest was 684.54 IU/mg in isolate CAT1.1.</p>
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Similar Papers
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.