Article Per Year (5 Year)
p-Index From 2021 - 2026
0.23
P-Index
This Author published in this journals
All Journal Jurnal Teknologi Dan Industri Pangan Jurnal Teknologi Industri Pertanian Microbiology Indonesia BIOTROPIA - The Southeast Asian Journal of Tropical Biology Indonesian Journal of Agricultural Science Jurnal AgroBiogen Jurnal Penelitian Pascapanen Pertanian Pengembangan Inovasi Pertanian Buletin Teknologi Pasca Panen agriTECH PROSIDING SEMINAR KIMIA BERITA BIOLOGI Informatika Pertanian Indonesian Journal of Chemistry Menara Perkebunan Pharmaceutical Sciences and Research (PSR) Amwaluna: Jurnal Ekonomi dan Keuangan Syariah
Nur Richana
Universitas Ibn Khaldun
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Economics, Econometrics & Finance Engineering Immunology & microbiology Industrial & Manufacturing Engineering Medicine & Pharmacology Veterinary

Published : 37 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 4 Documents
Search
Journal : BERITA BIOLOGI

 1 
KARAKTERISASI GEN PENYANDI PEDIOSIN PAF-11 PADA Pediococcus acidilactici F-11 [Characterization of the Pediocin PaF-11 Encoding Gene in Pediococcus acidilactici F-11] Marwati, Tri; Richana, Nur; Harmayani, Eni; Rahayu, Endang S
BERITA BIOLOGI Vol 11, No 2 (2012)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (299.137 KB) | DOI: 10.14203/beritabiologi.v11i2.495

Abstract

Pediocin PaF-11 is a ribosomally synthesized antimicrobial peptide produced by Pediococcus acidilactici F-11. The objectives of this research is to find out the location and the nucleotide sequence of gene, which is involved in the production of pediocin PaF-11. Results showed that the pediocin PaF-11 from the cured cell of P. acidilactici F-11 loss the activity, suggested that the pediocin PaF-11 gene was carried in the plasmid. Agarose gel electrophoresis of P. acidilactici F-11 plasmid DNA with marker λDNA/HindIII showed that pediocin PaF-11 gene was carried in 12 kb plasmid. Amplification pediocin PaF-11 gene from P. acidilactici F-11 showed that uncured P.acidilactici F-11 culture contain plasmid DNA, indicated by amplification of the papA gene (256 bp). Cured P. acidilactici F-11 culture, plasmid eliminated, indicted by no aplicon DNA detected. This result also suggested that pediocin PaF-11 gene in P. acidilactici F-11 was carried in plasmid. Nucleotide of pediocin PaF-11 encoding gene was sequenced The alignment of that nucleotide sequence showed that pediocin PaF-11 encoding gene have the same sequence with pediocin PA.1 encoding gene in P. acidilactici PAC1.0 and P. acidilactici K10 and pediocin AcH encoding gene in P. acidilactici LB 42-923 and P .parvulus ATO77, and pediocin CP2 in P. acidilactici MTCC 5101.
KARAKTERISASI DAN STUDI STABILISASI a-AMILASE Bacillus licheniformis TVII.6 MENGGUNAKAN BAHAN ADITIF Lestari, Puji; Richana, Nur; Rosmimik, Rosmimik
BERITA BIOLOGI Vol 10, No 5 (2011)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (400.712 KB) | DOI: 10.14203/beritabiologi.v10i5.1914

Abstract

The limited stability of enzyme during long-term storage attributes to its reduced function. In this study, a-amylase from Bacillus licheniformis TVII.6 were formulated with different kind of additives for storage stabilization and better performance. Simultaniously, some minerals and calcium ion were applied to elucidate the inhibition and activation effects to a-amylase. Crude enzyme which was prepared by aceton precipitation was used for this stability test. It demosntrated that 10% of mannitol in citrate phosphate buffer gave the highest residual activity after 3 months of storage (98.5%). Calcium ion influenced the thermal stability of a-amylase and it gave optimum activity at 5 mM CaCl , thus the stability increased from 76.0%/90 C/2 hours to 114.8%/90 C/22 hours in comparison without calcium ions. Calcium ions (5 mM CaCl ) on the stability of a-amylase at 4 C also produced the 2highest residual activity, which remained 100% during 48 hours of incubation. Chemical compounds like FeSO , Na CO and EDTA 4 2 3acted as inhibitors, while (NH ) SO , CuSO , CoSO , MgCl and K HPO did not inhibit activity of a-amylase. NaOH and MnCl 4 2 4 4 4 2 2 4 2 compounds at low concentrations (2 mM) did not inhibit the enzyme but at 10 mM became a-amylase inhibitors. This amylase stability information is very important as a consideration when applying and storing the enzyme, thereby reducing the degradation a-amylase activity.
KARAKTERISASI GEN PENYANDI PEDIOSIN PAF-11 PADA Pediococcus acidilactici F-11 Tri Marwati; Nur Richana; Eni Harmayani; Endang S Rahayu
BERITA BIOLOGI Vol 11, No 2 (2012)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v11i2.495

Abstract

Pediocin PaF-11 is a ribosomally synthesized antimicrobial peptide produced by Pediococcus acidilactici F-11. The objectives of this research is to find out the location and the nucleotide sequence of gene, which is involved in the production of pediocin PaF-11. Results showed that the pediocin PaF-11 from the cured cell of P. acidilactici F-11 loss the activity, suggested that the pediocin PaF-11 gene was carried in the plasmid. Agarose gel electrophoresis of P. acidilactici F-11 plasmid DNA with marker λDNA/HindIII showed that pediocin PaF-11 gene was carried in 12 kb plasmid. Amplification pediocin PaF-11 gene from P. acidilactici F-11 showed that uncured P.acidilactici F-11 culture contain plasmid DNA, indicated by amplification of the papA gene (256 bp). Cured P. acidilactici F-11 culture, plasmid eliminated, indicted by no aplicon DNA detected. This result also suggested that pediocin PaF-11 gene in P. acidilactici F-11 was carried in plasmid. Nucleotide of pediocin PaF-11 encoding gene was sequenced The alignment of that nucleotide sequence showed that pediocin PaF-11 encoding gene have the same sequence with pediocin PA.1 encoding gene in P. acidilactici PAC1.0 and P. acidilactici K10 and pediocin AcH encoding gene in P. acidilactici LB 42-923 and P .parvulus ATO77, and pediocin CP2 in P. acidilactici MTCC 5101.
KARAKTERISASI DAN STUDI STABILISASI a-AMILASE Bacillus licheniformis TVII.6 MENGGUNAKAN BAHAN ADITIF Puji Lestari; Nur Richana; Rosmimik Rosmimik
BERITA BIOLOGI Vol 10, No 5 (2011)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v10i5.1914

Abstract

The limited stability of enzyme during long-term storage attributes to its reduced function. In this study, a-amylase from Bacillus licheniformis TVII.6 were formulated with different kind of additives for storage stabilization and better performance. Simultaniously, some minerals and calcium ion were applied to elucidate the inhibition and activation effects to a-amylase. Crude enzyme which was prepared by aceton precipitation was used for this stability test. It demosntrated that 10% of mannitol in citrate phosphate buffer gave the highest residual activity after 3 months of storage (98.5%). Calcium ion influenced the thermal stability of a-amylase and it gave optimum activity at 5 mM CaCl , thus the stability increased from 76.0%/90 C/2 hours to 114.8%/90 C/22 hours in comparison without calcium ions. Calcium ions (5 mM CaCl ) on the stability of a-amylase at 4 C also produced the 2highest residual activity, which remained 100% during 48 hours of incubation. Chemical compounds like FeSO , Na CO and EDTA 4 2 3acted as inhibitors, while (NH ) SO , CuSO , CoSO , MgCl and K HPO did not inhibit activity of a-amylase. NaOH and MnCl 4 2 4 4 4 2 2 4 2 compounds at low concentrations (2 mM) did not inhibit the enzyme but at 10 mM became a-amylase inhibitors. This amylase stability information is very important as a consideration when applying and storing the enzyme, thereby reducing the degradation a-amylase activity.
Co-Authors A.A. Ketut Agung Cahyawan W Abdullah Bin Arif Abdullah bin Arif Achmad Zainudin Agus Budiyanto Agus Budiyanto Anja Meryandini Anwar Nur Anwar Nur Arif SP.MSi, Abdullah Bin Arif, Abdullah bin Budiyanti, Agus Budiyanto, Agus Christina Winarti Darwis, Abdul Aziz Dedi Fardiaz Diyono, Wahyu Diyono, Wahyu Djumali Mangunwidjaja Djumali Mangunwidjaja Dwi Setyaningsih EKA RURIANI Eka Ruriani Endang Prangdimurti Endang S Rahayu Endang S Rahayu Eni Harmayani Eni Harmayani Enrico Syaefullah Erliza Noor Evi Savitri Iriani Faizal Gayang Firda DIMAWARNITA Hanny Hafiar Hayuningtyas, Maulida I Ketut Suada I Wayan Arnata Illah Sailah Irfan Syauqi Beik Irinne D.P Khaswar Syamsu Lestari, Puji M. ANWAR NUR MARIA BINTANG Maulida Hayuningtyas Munarso, S. Joni Murdiyatmo, Untung nFN Suliantari nFN Widaningrum Nurhayati, Immas Puji Lestari PUJI LESTARI Puji Lestari Purwiyatno Hariyadi Rahmawati Rahmawati Ratih Dewanti -Hariyadi Ratnaningsih Ratnaningsih Ribowo, Sugeng Rina Masriani Rosmimik Rosmimik Rosmimik, Rosmimik Sakae Suzuki SOFIYANTO, M. EDY Sri Laksmi Suryaatmadja Sri Usmiati Suharyanto Titi C Sunarti Titi C. Sunarti Titi Candra Sunarti Titi Chandra Sunarti Tri Marwati Tri Marwati Tri Marwati Tri Panji Tun T. Irawadi Tun Tedja Irawadi Wahyu Diyono Wahyu Diyono Yandra Arkenan Yoshiharu Fujii