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All Journal HAYATI Journal of Biosciences Microbiology Indonesia Jurnal Bioteknologi & Biosains Indonesia (JBBI)
IS HELIANTI
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Earth & Planetary Sciences Environmental Science Health Professions Immunology & microbiology Medicine & Pharmacology

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Gene Cloning of Xylanase Glycoside Hydrolase Family 11 from Bacillus halodurans CM1 in Escherichia coli DH5α Muhamad Taufiqul Naufal; Agustin Krisna Wardani; IS HELIANTI
Microbiology Indonesia Vol. 13 No. 4 (2019): December 2019
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2549.245 KB) | DOI: 10.5454/mi.13.4.3

Abstract

Xylanase is an enzyme that can break down xylan into xylose and xylooligosaccharide that is widely used in industry. Seeing the many applications of this enzyme, researchers conducted many studies on how to increase the productivity and effectiveness of the xylanase enzyme. One of the method that can be used to increase the xylanase enzyme production process is by using recombinant DNA technology such as cloning. Bacillus halodurans CM1 is a local alkalothermophilic bacterium that potential producer for xylanase and other industrial enzymes. This research was conducted to clone the GH11 xylanase coding gene from B. halodurans CM1 using pJET 1.2 / blunt plasmid as vector into Escherichia coli DH5α as cell host and  determine the nucleotide base sequence of the GH11 xylanase coding gene from B. halodurans CM1. The results showed the GH11 xylanase gene from B. halodurans CM1 was successfully cloned in  E. coli DH5α and based on the results of BLAST nucleotides had 99% similarities with that of endo-1,4-beta -xylanhydrolase (xyn11A) from B. halodurans C-125. Key words: Bacillus halodurans CM1, cloning, xylanase glycoside hydrolase family 11
The utilization of auto-inducible Plyb promoter and media optimation for cell density-dependent expression of recombinant xylanase in Bacillus subtilis DB104 Haniyya Haniyya; Dini Achnafani; Maria Ulfah; Niknik Nurhayati; Is Helianti
Microbiology Indonesia Vol. 14 No. 1 (2020): March 2020
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1582.039 KB) | DOI: 10.5454/mi.14.1.2

Abstract

Strong promoters are one of the fundamental aspects to increase the level of gene expression, and one of approach to improve the recombinant enzyme productivity so that the efficiency of production cost for enzyme production in industrial scale can be reached. Here we assessed the application of a cell density-dependent promoter and media optimation to promote cell growth and protein expression of Bacillus subtilis without excess usage of inducers. An auto-inducible Pylb promoter that is potential to provide inducer-free enzyme production was cloned and introduced into xylanase recombinant system in B. subtilis DB104 by PCR cloning and protoplast transformation. A 200 bp target gene was successfully inserted in between xynCM1 ORF -coding for B. halodurans CM1 xylanase- and its native promoter sequence at the upstream region. The disruption of the native promoter was intended to replace the native promoter with Pylb. Recombinant xylanase gene under Pylb was successfully expressed in B. subtilis DB104 and the enzyme was produced at stationary phase. Different media with various concentrations of glucose and nitrogen were used to optimize recombinant xylanase expression. It achieved a higher level of xylanase expression compared to wild-type and recombinant xylanase with native promoter B. subtilis in media containing a 2-fold recipe of LB media thus leads to increase cell density and xylanase expression (81.461 U mL-1).
Production and Characterization of Thermoalkaliphilic Xylanase from Bacillus halodurans CM1 on Degumming Process of Ramie (Boehmeria nivea L.Gaud)Fiber as Textile Raw Material DEWI NANDYAWATI; DEA INDRIANI ASTUTI; NIKNIK NURHAYATI; ASEP RISWOKO; IS HELIANTI
Microbiology Indonesia Vol. 15 No. 3 (2021): September 2021
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (972.873 KB) | DOI: 10.5454/mi.15.3.3

Abstract

Ramie fiber is a potential raw material to substitute imported raw materials such as cotton. Due to its higher hemicellulose content, ramie fiber required hydrolysis in a process called degumming. Enzymatic degumming is environmentally friendly compared to traditional process which using chemicals. Alkalithermophilic xylanase have high ability in hemicellulose hydrolysis. The production of xylanase was conducted by submerged fermentation of Bacillus halodurans CM1 in 20L bioreactor using Mamo and corncob medium with optimum conditions at 50°C, pH 9, 150 RPM and 1 vvm. The optimum specific activity of xylanase measured by Bailey method at 70°C and pH 9 is 475.41 U/mg. Xylanase was stable at 50°C, pH 9 and relatively stable to K+, Na2+, Co2+ and Ca2+ metal ions and Triton-X, Saba dan Tween-80 surfactants. Degumming process was carried out by immersing ramie fibers in formulated degumming solution with vlot 1:20 at 50°C, 150 RPM and 180 minutes. The enzymatic degumming process may substitute or reduce the use of chemicals due to its significant effect on ramie fiber quality. Enzymatic and chemical degumming process reduce the weight of Ramie Fiber to 7.23 %, and 7.72 %, slightly higher than enzymatic degumming 7.15%. Enzymatic degumming maintains tensile strength at 27.51 %. Whiteness index enhanced to 2.99% enzymatically and 3.49% chemically. Keywords: Bacillus halodurans CM1, enzymatic degumming, ramie fiber, textile industry, thermoalkaliphilic xylanase
APPLICATION OF RECOMBINANT TRIACYLGLYCEROL LIPASE AND CARBOXYLESTERASE ENZYMES FROM Bacillus velezensis STRAIN S3 FOR POLYESTER SURFACE MODIFICATION Is Helianti
Jurnal Bioteknologi dan Biosains Indonesia Vol. 9 No. 2 (2022)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

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Abstract

Enzymatic polyester surface modification can be performed with lipase and esterase enzymes. In this study, the polyester fabric modification utilized triacylglycerol lipase (TGA) and carboxylesterase (CES) recombinant enzymes. The effect of these treatments was observed by determining the hydrophilicity level, dye absorption level, hydroxyl group measurement, and fiber surface morphology. The results revealed an elevated hydrophilicity level in polyester fabric, followed by dye absorption improvement and carboxyl group increase. The water absorption times required by the fabric based on the results of TGA, CES, comparative lipase, and negative control treatments were 3±0.05 seconds, 3.5±0.07 seconds, 5±0.05 seconds, and 80±11.54 minutes, respectively. Dye absorption test in polyester fabric based on these groups mentioned above were 52±0.5, 58±0.5, 178±0.5, and 2968±290 seconds. The total hydroxyl group measurement in polyester fabric was observed at 30.9±0.09, 30.5±0.05, 28.6±0.09, and 3 meq/100 g. The SEM observation showed that the enzymatic hydrolysis could alter the porous structure and surface of the fibers.
INCREASING RECOMBINANT PENICILLIN G ACYLASE PRODUCTION: GENETIC, PROTEIN ENGINEERING, AND PRODUCTIVITY IMPROVEMENT Is Helianti
Jurnal Bioteknologi dan Biosains Indonesia Vol. 9 No. 2 (2022)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

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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.
Co-Authors . KOESNANDAR AA Sudharmawan, AA Abinawanto Abinawanto AGUSTIN KRISNA WARDANI Ani Suryani ASEP RISWOKO ASTUTIATI NURHASANAH Budiasih Wahyuntari Dea Indriani Astuti DEWI NANDYAWATI Dini Achnafani DWI SURYANTO FENTRI PARAMITHA PUTRI Haniyya Haniyya Joni Kusnadi Khaswar Syamsu Lisa Pratama LLINA MULYAWATI MILANI ANGGIANI Mochamad Nurcholis Muhamad Taufiqul Naufal NIKNIK NURHAYATI RIMA AZARA Sara Gustia Wibowo SHANNI FERNANDA TATI NURHAYATI