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All Journal Bioma : Berkala Ilmiah Biologi Bioma : Jurnal Ilmiah Biologi
Hasibuan, Imron Martua
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Education Immunology & microbiology

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ISOLATION OF AnsB GENE FRAGMENT ENCODING L-ASPARAGINASE 2 ENZYME FROM Serratia plymuthica UBCF_13 AND IT’S IN-SILICO DOMAIN CHARACTERISTIC Ananda, Abi Awfa Rahman; Nursyafi, Fauzan Syarif; Aliya, Lisana Shidiqqin; Hasibuan, Imron Martua; Alioes, Yustini; Endrinaldi , Endrinaldi; Adrial, Adrial; Elmatris , Elmatris; Jamsari, Jamsari; Lily Syukriani
BIOMA : Jurnal Ilmiah Biologi Vol. 14 No. 1 (2025): April 2025
Publisher : Prodi Pendidikan Biologi, FPMIPATI, Universitas PGRI Semarang

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.26877/n5mfhy69

Abstract

Acute lymphoblastic leukemia(ALL) is one of the cancer diseases often occurs in children and causes high mortality in children. One of the chemotherapy treatment suggested is using L-Asparaginase 2. However due to its difficult production process making this approach expensive for the public. Therefore production technology of this enzyme is crucial enabling cheaper for ALL treatment. This study aimed to isolate the AnsB gene sequence from Serratia plymuthica UBCF_13 and perform its further in-silico analysis. The research was started by designing specific primers for the AnsB gene, isolating the AnsB gene fragment using PCR-based approach, sequencing the AnsB gene fragment, cloning the fragment to the plasmid vector and further transformed into E. coli DH5α cell. Further data analysis was carried out using some bioinformatics tools such as BLAST, MEGA X, I-TASSER InterPro. Sequence data result successfully verified that the full length of AnsB gene is 1047 bp. InterPro analysis indicated that the L-Asparaginase 2 from S. plymuthica UBCF_13 has 2 domains, namely L-Asparaginase N-terminal spanning from amino acid 26 to 216, while its C-terminal spanned from amino acid 235 to 345. The physical fragment of the gene was also successfully cloned to the pGEM-T Easy vector and subsequently transformed into E. coli DH5α cell. This result provided information for alternative sources of L-Asparaginase 2 and it’s possible engineering.
Enhanced expression of L-asparaginase II by fusion of pSSPM3 synthetic promoter into pET-28a+ expression vector for alternative targeted therapy of acute lymphoblastic leukaemia Aliya, Lisana Shiddiqin; Julizar, Julizar; Rasyid, Roslaili; Pertiwi, Dian; Syukriani, Lily; Nursyafi, Fauzan Syarif; Saibi, Ihsan R. A.; Hasibuan, Imron Martua; Febiona, Keysha Putri; Jamsari, Jamsari
Bioma : Berkala Ilmiah Biologi Volume 27 Issue 2 Year 2025
Publisher : Departemen Biologi, Fakultas Sains dan Matematika, Universitas Diponegoro

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14710/bioma.2025.72304

Abstract

The use of commercial L-asparaginase II from E. coli and Erwinia chrysanthemi for acute lymphoblastic leukemia (ALL) therapy causes adverse effects (allergic reactions, neurotoxicity), necessitating safer alternatives. Serratia plymuthica UBCF_13, harboring the ansB gene, offers a promising source. This study constructed the recombinant plasmid pET-28a+:pSSPM3:ansB to enhance L-asparaginase II expression in E. coli using the synthetic promoter pSSPM3. Molecular verification confirmed successful steps: promoter fusion (674 bp band), ansB digestion (1,057 bp), gene insertion (1,682 bp), and BL21 transformation. Critically, enzyme activity assays revealed that pSSPM3 did not enhance expression in BL21 (0.519 U/mL), showing significantly lower activity (p<0.05) than native controls (0.621 U/mL) and DH10B transformants (0.636 U/mL). While the functional plasmid establishes a platform for novel enzyme production, the unexpected activity reduction in BL21 and higher yield in DH10B highlight host-promoter compatibility challenges. Further optimization of expression systems, purification protocols, and preclinical validation (cytotoxicity, allergenicity) are essential to advance this recombinant enzyme toward therapeutic and scalable industrial applications for ALL in resource-limited settings.
Co-Authors Adrial Adrial, Adrial Aliya, Lisana Shiddiqin Aliya, Lisana Shidiqqin Ananda, Abi Awfa Rahman Dian Pertiwi Elmatris Sy Endrinaldi , Endrinaldi Febiona, Keysha Putri Jamsari Jamsari Julizar Julizar Lily Syukriani Nursyafi, Fauzan Syarif Roslaili Rasyid Saibi, Ihsan R. A. Yustini Alioes