Article Per Year (5 Year)
p-Index From 2020 - 2025
2.255
P-Index
This Author published in this journals
All Journal Bioscience Biogenesis: Jurnal Ilmiah Biologi BERITA BIOLOGI Jurnal Bioteknologi & Biosains Indonesia (JBBI) BIOEDUKASI ANNALES BOGORIENSES Jurnal Pengabdian Masyarakat AbdiMas Biofarm : Jurnal Ilmiah Pertanian SPIN: Jurnal Kimia & Pendidikan Kimia Jurnal Pengabdian kepada Masyarakat Annales Bogorienses
Febriana Dwi Wahyuni
Universitas Esa Unggul
Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Economics, Econometrics & Finance Education Environmental Science Immunology & microbiology Languange, Linguistic, Communication & Media Library & Information Science Medicine & Pharmacology Public Health Social Sciences Other

Published : 19 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 2 Documents
Search
Journal : ANNALES BOGORIENSES

 1 
Constitutive Expression of Candida antarctica Lipase B (CALB) in Pichia pastoris Using pGAPZα Vector Wahyuni, Febriana Dwi; Fuad, Asrul Muhamad; Suharsono, Suharsono
ANNALES BOGORIENSES Vol 20, No 1 (2016): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (461.586 KB) | DOI: 10.14203/ab.v20i1.225

Abstract

The CalBsyn gene was previously constructed synthetically to encode Candida antarctica lipase B (CALB). Lipase from CalBsyn gene is slightly different from that of wild type CALB (CALB-wt) where it has three amino acids substitutions at different positions, i.e. V210I, A281E, and V221D, to improve enzyme’s thermostability and catalytic efficiency. The CalBsyn gene was isolated from pJ912-CalBsyn vector by digestion using XhoI restriction enzyme. The CalBsyn gene then was ligated to pGAPZα expression vector and transformed into E. coli TOP10F’ in order to obtain recombinant vector pGAPZα-CalBsyn. The result showed that pGAPZα-CalBsyn recombinant vector was successfully transformed into E. coli TOP10F’ with transformation efficiency of 4.11 x 103 cfu/µg plasmid DNA. The pGAPZα-CalBsyn recombinant plasmid was successfully introduced into Pichia pastoris SMD1168H using electroporation method with transformation efficiency of 1.01 x 102 cfu/µg DNA. Qualitative lipase activity assays showed that transformed P. pastoris secreted recombinant lipase (CALB) and has lipolytic activity; while quantitative lipase activity assays showed that the lipase activity was 63.5 Units/ml in 48 hours. Analysis using SDS-PAGE showed that CALB protein was expressed successfully and the recombinant protein’s molecular size was approximately 45 kDa.
Constitutive Expression of Candida antarctica Lipase B (CALB) in Pichia pastoris Using pGAPZα Vector Febriana Dwi Wahyuni; Asrul Muhamad Fuad; Suharsono Suharsono
ANNALES BOGORIENSES Vol 20, No 1 (2016): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (461.586 KB) | DOI: 10.14203/ann.bogor.2016.v20.n1.31-38

Abstract

The CalBsyn gene was previously constructed synthetically to encode Candida antarctica lipase B (CALB). Lipase from CalBsyn gene is slightly different from that of wild type CALB (CALB-wt) where it has three amino acids substitutions at different positions, i.e. V210I, A281E, and V221D, to improve enzyme’s thermostability and catalytic efficiency. The CalBsyn gene was isolated from pJ912-CalBsyn vector by digestion using XhoI restriction enzyme. The CalBsyn gene then was ligated to pGAPZα expression vector and transformed into E. coli TOP10F’ in order to obtain recombinant vector pGAPZα-CalBsyn. The result showed that pGAPZα-CalBsyn recombinant vector was successfully transformed into E. coli TOP10F’ with transformation efficiency of 4.11 x 103 cfu/µg plasmid DNA. The pGAPZα-CalBsyn recombinant plasmid was successfully introduced into Pichia pastoris SMD1168H using electroporation method with transformation efficiency of 1.01 x 102 cfu/µg DNA. Qualitative lipase activity assays showed that transformed P. pastoris secreted recombinant lipase (CALB) and has lipolytic activity; while quantitative lipase activity assays showed that the lipase activity was 63.5 Units/ml in 48 hours. Analysis using SDS-PAGE showed that CALB protein was expressed successfully and the recombinant protein’s molecular size was approximately 45 kDa.
Co-Authors Adri Nora alfero Putra Iryanto Anisa Febriyanti Asrul Muhamad Fuad Asrul Muhamad Fuad Asrul Muhamad Fuad, Asrul Muhamad callista marsya Dedi Supriadi Dimas Ridho Irvansah Enung Sri Mulyaningsih feby feby Hani Fitriani, Hani Henny Saraswati Henny Saraswati Iis Nur Asyiah Kartika Sari Dewi Kevin Febrianus Moda Meisya Then Septian Muhamad Amza Sidiq nie nie Ningsih, Irnawati Novianti, Titta Novita Sari Oktaviani Naulita Turnip putri mega utami Rahman, Nurhamidar roaslein putri Roselein Putri sabar pambudi Saraswati, Henny Saraswati, Henny Seprianto, Seprianto Slamet Hariyadi Sri Rianawati Suharsono Suharsono Suharsono Suharsono Syafruddin Ilyas