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All Journal HAYATI Journal of Biosciences Bioma : Berkala Ilmiah Biologi Indonesian Journal of Biotechnology Berkala Bioteknologi Makara Journal of Science Jurnal Bioteknologi & Biosains Indonesia
IS HELIANTI
Center for Bioindustrial Technology, Laboratorium of Bioindustrial Technology, LAPTIAB BPPT Puspiptek -Serpong
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Earth & Planetary Sciences Education Immunology & microbiology Materials Science & Nanotechnology

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INCREASING RECOMBINANT PENICILLIN G ACYLASE PRODUCTION: GENETIC, PROTEIN ENGINEERING, AND PRODUCTIVITY IMPROVEMENT Helianti, Is
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol. 9 No. 2 (2022)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/jbbi.2022.1775

Abstract

B-lactam derived antibiotics are the most used globally for treatment against different infections caused by pathogenic bacteria and comprises 65% of the world antibiotics. Recently, penicillin G acylase (PGA) is used as biocatalyst for those B-lactam antibiotics production by which 6-aminopenicillanic acid (6-APA) or 7-aminodeacetoxycephalosporanic acid (7-ADCA) as the building blocks is produced. Commercialized PGA from native microbial resources are still limited to E. coli. Therefore, genetic engineering approach such as cloning and expression in other microbial hosts were assessed to enhance bacterial strains that produce PGA. However, such improvement could increase immature precursors accumulation and lowering the enzyme yield, activity, or stability. This review focus on the review of PGA recombinant produced by several microbial host, their expression levels, and improvement achieved by some modification such as replacement of signal peptide and promoter continued to protein engineering to utilize the enzymes in synthetizing amoxicillin rather than to hydrolyses Penicillin G.
A Comparative Study of Penicillin G Acylase Expression in Two Escherichia coli Strains: BL21 (DE3) and Arctic Express Cendana, Kartika Sari; Wulandari, Sri Rezeki; Sabbathini, Gabriela Christy; Ulfah, Maria; Achnafani, Dini; Abinawanto; Aniqah, Sunni Sofiah; Helianti, Is; Nurhayati, Niknik
HAYATI Journal of Biosciences Vol. 33 No. 3 (2026): May 2026
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.33.3.596-604

Abstract

The growing demand for semisynthetic beta-lactams has directed attention towards enzymes, specifically Penicillin G Acylases (PGAs), for their potential in synthesizing these antibiotics. This study delves into the expression of Achromobacter xylosoxidans PGA (AxPGA) in Escherichia coli, with a focus on enhancing the yield of active PGA, often constrained by a complex maturation process. The optimization of PGA expression included variations in IPTG concentration and the addition of CaCl2. Furthermore, the study compared PGA expression in E. coli BL21 (DE3) with that in E. coli Arctic Express (DE3), capable of co-expressing chaperones (chaperonin Cpn60 and Cpn10). Induction with 0.5 mM IPTG resulted in the highest hydrolytic activity in both strains, with Arctic Express (AE) exhibiting significantly higher activity due to improved folding facilitated by cold-adapted chaperonins. Alongside optimal IPTG induction, the addition of 10 mM CaCl2 in the culture media significantly increased PGA activity in both strains, highlighting that Ca2+ supplementation is an effective strategy to enhance the yield of functional PGA. Subcellular fractionation demonstrates that the periplasmic fraction yielded higher volumetric and specific activities compared to the cytoplasmic fractions in both E. coli strains, highlighting the importance of periplasmic processing for PGA maturation. This suggests that extracting the periplasmic fraction is an effective strategy for recovering active PGA while avoiding or reducing contamination either from co-expressed cytoplasmic chaperones or other intracellular proteins. These findings emphasize that induction strategy, ionic stabilization, and host strain selection play synergistic roles in increasing active recombinant PGA expression.
Detection of homologous plastic PET‐degrading enzyme‐encoding DNA from enriched plastic‐contaminated soil samples Wulandari, Sri Rezeki; Sabbthini, Gabriela Christy; Trinugroho, Joko Pebrianto; Nurhayati, Niknik; Ulfah, Maria; Helianti, Is
Indonesian Journal of Biotechnology Vol 31, No 1 (2026)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.112331

Abstract

Piscinibacter sakaiensis, first isolated in Japan, is the only well‐characterized bacterium known to possess both PETase and MHETase, enabling complete polyethylene terephthalate (PET) degradation. To date, no additional habitats for the species have been reported. This study aims to identify homologous PETase and MHETase DNA from plastic‐contaminated landfill soils in Indonesia. Enrichment cultures were established from soil samples collected at Galuga (Bogor) and Cipeucang (South Tangerang). PCR amplification and sequencing revealed a full‐length MHETase homolog (G2MHETase, 1,812 bp) from Galuga, showing 99.4% and 99.3% nucleotide identity to MHETase from P. sakaiensis and Delftia sp. respectively. The deduced amino acid sequence shared 98.5% identity with both. In contrast, a partial PETase homolog (502 bp of 873 bp) was amplified from the Cipeucang sample, displaying 96 and 93% amino acid identity to PETase from P. sakaiensis and P. gummiphilus respectively. Nanophore NGS analysis of bacterial diversity indicated distinct microbial community profiles between the two sites. Rare taxa potentially associated with the detected genes included P. gummiphilus, Delftia sp., Delftia tsuruhatensis and Xenophilus aerolatus from Galuga, and Piscinibacter and Acidovorax from Cipeucang. These findings demonstrate the feasibility of detecting homologous PET degrading enzyme genes from plastic‐contaminated soils using PCR‐based approaches.
Co-Authors Abinawanto Abinawanto Abinawanto Achnafani, Dini AGUSTIN KRISNA WARDANI Ahmad Wibisana, Ahmad Ajrullah, Mauludy Jutta Amarila Malik Aniqah, Sunni Sofiah Anto Budiharjo Cendana, Kartika Sari Dini, Muthia Rahmah Fatiningtyas, Fairuz Andini Feronika Heppy Sriherfyna Furgeva, Natasha Gunawan, Ellen Fenix Hermin Pancasakti Kusumaningrum I Gede Eka Perdana Putra, I Gede Eka Perdana K, Hermin Pancasakti KHOMAINI HASAN Maria Ulfah Masdalifah, Masdalifah Mochamad Nurcholis Mulyawati, Lina Napitupulu, Riswanto Nataniel, Jocelyn NIKNIK NURHAYATI Pramesti, Nadya Shafa Prawiro, Sumarno Reto Rejeki Siti Ferniah Sabbathini, Gabriela Christy Sabbthini, Gabriela Christy Safirah, Dearesty Tri Yudani MR Trinugroho, Joko Pebrianto Wulandari, Sri Rezeki