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Ifa Manzila
Balai Besar Penelitian dan Pengembangan Bioteknologi dan Sumberdaya Genetik Pertanian Jl. Tentara Pelajar No.3A Cimanggu Bogor 16114
Agriculture, Biological Sciences & Forestry Medicine & Pharmacology

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Konjugat Poliklonal Antibodi Nanopartikel Emas untuk Deteksi Potato Virus Y Ifa Manzila; Tri Puji Priyatno; Fikri Hidayatullah
Jurnal Fitopatologi Indonesia Vol 16 No 2 (2020)
Publisher : The Indonesian Phytopathological Society (Perhimpunan Fitopatologi Indonesia)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14692/jfi.16.2.87-93

Abstract

Polyclonal Antibodi-Gold Nanoparticles for Potato Virus Y Detection Gold nanoparticles are stable colloidal solutions with dimensions of 1-100 nm having surface plasmon resonance with six free electrons. The existing of six free electrons on the surface of a plasmon causes gold nanoparticles to bind easily to various types of bioreseptors including polyclonal antibodies. Polyclonal potato virus Y (PVP) antibodi been successfully conjugate with gold nanoparticles in order to develop a rapid detection for PVY infection in potato plants. The gold nanoparticles was synthetized by the reduction of gold (III) chloride trihydrate (HAuCl4) with 1% sodium citrate. Subsequently, the nanoparticles were used to make gold nanoparticle-antiobody PVY-conjugate. PVY detection was carried out with dot blot method on the nitrocellulose membrane. The results showed that the PVY virus on the membrane can be detected 10-30 minutes after incubation, depend on the concentration of the conjugate and the concentration of the virus in the sampel. The use of gold nanoparticle conjugates can increase the efficiency of the immunodot blot method in about 1 hour, and this method can be developed to be a lateral flow system for field detection of PVY.
Expression and Characterization of Recombinant β-1,3-Glucanase of Burkholderia cepacia (BiogenCC E76) Expressed in Escherichia coli Expression Systems Tri Puji Priyatno; Fitriani Winangsih; Ifa Manzila; Maria Bintang
Jurnal AgroBiogen Vol 15, No 1 (2019): June
Publisher : Balai Besar Penelitian dan Pengembangan Bioteknologi dan Sumber Daya Genetik Pertanian

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21082/jbio.v15n1.2019.p35-44

Abstract

Burkholderia cepacia (Bcc) BiogenCC E76 isolate is an endophytic bacterium producing cell wall degrading enzyme, glucanase, and antagonistic to fungal pathogens, such as Magnaporte grisea and Colletotrichum gloeosporioides. The glucanase is able to lyse fungal cell walls composed of glucan causing disintegrity of mycelia and fungi fail to infect plants. The purpose of this study was to clone, express, and characterize 48 kDa subunit of β-1,3-glucanase from Bcc isolate BiogenCC E76 using the Escherichia coli expression system. The 1,300 bp of the β-1,3-glucanase gene was constructed using the pET-32b vector in BamHI-HindIII restriction sites to generate the pET-Glu plasmid. The gene was fused with nucleotides sequence encoding Trx-tag, His-tag, and S-tag producing 65 kDa of recombinant β-1,3-glucanase. Gene expression in the construct was controlled by the T7 promoter and Trx-tag start codon through IPTG induction. The recombinant β-1,3-glucanase was then purified and its activities were tested at different pH and temperature conditions. Results showed that E. coli carrying pET-Glu overexpressed a 65 kDa protein in induced culture as a soluble protein that was expressed in periplasm. Purification result of the crude extract of the recombinant protein obtained 27% pure enzymes with a specific activity of 1,207.976 U/mg and purity level of 3.9 fold. This recombinant glucanase demonstrated optimal activity at 40°C and pH 5–7. A deeper study is needed to understand the role of 48 kDa subunit of β-1,3-glucanase has in antagonistic mechanism of Bcc against pathogenic fungi.
Co-Authors Fikri Hidayatullah Fitriani Winangsih MARIA BINTANG Tri Puji Priyatno Tri Puji Priyatno