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All Journal Berkala Bioteknologi Makara Journal of Science
Furgeva, Natasha
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Biochemistry, Genetics & Molecular Biology

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Cloning of a Gene Encoding Protease from Bacillus halodurans CM1 into Escherichia coli DH5α and Expression Analyses of the Gene Product Helianti, Is; Furgeva, Natasha; Mulyawati, Lina; Ferniah, Rejeki Siti; Kusumaningrum, Hermin Pancasakti
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Bacillus halodurans strain CM1 is an Indonesia alkalothermophilic bacterium isolated from Cimanggu Hot Spring, Bandung, West Java. This bacterial strain produces high levels of thermoalkalophilic xylanase. It has also been predicted to produce other potential industrial enzymes, including protease. For production and application of protease in the future, the protease gene from B. halodurans CM1 was cloned into Escherichia coli. The protease gene was isolated from B. halodurans CM1 by the PCR approach using primers designed based on the GenBank. The PCR product was then ligated into pGEM-T Easy vector, transformed into E. coli DH5α, verified, and analyzed based on DNA sequencing data using the BLAST search tool. A 1086-bp protease gene was obtained that exhibited a very high sequence similarity (99%) with that of alkaline protease gene from B. halodurans C-125. When the culture of this positive recombinant E. coli DH5α containing the protease gene was spotted onto calcium caseinate agar, a clear zone appeared after incubation at 50 °C. This result demonstrated that the protease gene was expressed in this recombinant E. coli DH5α.
Cloning of A Gene Encoding Protease from Bacillus halodurans CM1 into Escherichia coli DH5α Furgeva, Natasha; Helianti, Is; Ferniah, Rejeki Siti; K, Hermin Pancasakti
Berkala Bioteknologi Vol. 4, No. 2, November 2021
Publisher : Berkala Bioteknologi

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Bacillus halodurans strain CM1 was an Indonesia alkalothermophilic bacteria isolated from Cimanggu Hot Spring, Bandung, West Java. The activity of alkalo thermophilic protease enzyme from B. halodurans CM1 was detected. Nowadays, alkalothermophilic protease enzyme was applied for the eco-friendly industrial purpose, for example, as additive substance in detergent product. For the production and application of protease in the future, the cloning of protease gene from B. halodurans CM1 into E. coli was conducted. The protease gene was isolated from B. halodurans by PCR approach using primers designed based on the GenBank database. The PCR product then ligated into pGEM-T Easy vector, transformed into Escherichia coli DH5α, verified, and analyzed using DNA sequencing and bioinformatic tools BLAST. The results showed that 1086 bp protease gene was obtained and had 99% similarity with that of alkalostable protease from B. halodurans C-125. When the culture of this positive recombinant E. coli DH5α containing the protease gene spotted onto calcium caseinate agar, the clear zone appeared after incubation at 50 °C. It showed that the protease gene was expressed in this recombinant E.coli DH5α.
Co-Authors Hermin Pancasakti Kusumaningrum IS HELIANTI K, Hermin Pancasakti Mulyawati, Lina Rejeki Siti Ferniah