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Makara Journal of Science
Published by Universitas Indonesia
ISSN : 23391995     EISSN : 23560851     DOI : https://doi.org/10.7454/mss
Core Subject :
Makara Journal of Science publishes original research or theoretical papers, notes, and minireviews on new knowledge and research or research applications on current issues in basic sciences, namely: Material Sciences (including: physics, biology, and chemistry); Biochemistry, Genetics, and Molecular Biology (including: microbiology, physiology, ecology, taxonomy and evolution); and Biotechnology.
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Articles 7 Documents
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Search results for , issue "Vol. 22, No. 3" : 7 Documents clear
Characterization of Protease from Bacillus licheniformis F11.1 as a Bio-Detergent Agent lmiah, Sitti Nur; Mubarik, Nisa Rachmania; Wahyuntari, Budiasih
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

Proteases are among the most important enzymes in both food and non-food industries taking up almost 60% of the world enzyme market. This enzyme has been used for many industrial processes, especially in the detergent industry. The purpose of this study was to characterize the protease from Bacillus licheniformis F11.1 as a bio-detergentagent. An enzyme assay of protease activity was used to assess and characterize the protease enzyme from B. licheniformis F11.1. It showed that the highest pH protease activity for alkaline protease occurred at pH 8.0 with a value of 35.00U/mL. Under incubation temperature, the protease had the highest activity at 50 °C with a value of 24.46 U/mL. Protease activity was inhibited by Ca2+,Mn2+, K+, and Na+ions at concentrations of 5 mM. Protease activity can beenhanced by these ions at concentrations of 2 mM. Protease stability can be measured from half-life. Under anincubation temperature of 50 °C, the half-life of the protease at pH 8, 9, and 10 was 108 min, 114 min, and 98 min, respectively. The assay for enzyme stability with an incubation temperature of 60 °C showed half-lives of 92 minutes, 56 minutes, and 61 minutes for pH 6, 9, and 10, respectively. This enzyme was found to be stable with the addition ofdetergent compounds such as sodium dodecyl sulfate (SDS), Triton X-100, ethylenediaminetetraacetic acid (EDTA), and hydrogen peroxide; all under low concentrations. Determination of the molecular weight using SDS-PAGE andzymogram found the molecular weight was 32.90-35.16 kDa. These results showed that the alkaline protease from B.licheniformis F11.1 can be used as a bio-detergent because of its tolerance to various detergent compounds.
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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Abstract

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.
Isolation and Characterization of Cellulose from Underexploited Golden Melon Skin Adewuyi, Adewale; Pereira, Fabiano Vargas
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

Golden melon skin (GM) is an underexploited plant resource in Nigeria from which cellulose (GMC) was isolated and characterized. Characterization was achieved using Fourier transform-infrared (FT-IR) spectroscopy, X-ray diffraction (XRD), thermogravimetric analysis, and scanning electron microscopy. GMC was further evaluated for its water holding capacity (WC), oil holding capacity (OC), water swelling capacity (SC), and heavy metal adsorption capacity. FT-IR spectroscopy revealed peaks correspondingto GMC, while the XRD diffraction planes exhibited by GMC were typical of cellulose I crystals with a crystallinity index of 40%. The thermal degradation of GMC revealed a first mass loss at 190–295 °C, second loss at 305–410 °C, and third loss 285–430 °C. The WC was 11.62 g/g, OC was 2.75 mL/g, and SC was 9.32 mL/g. The heavy metal adsorption capacity of GMC toward Cu (II) was 34.52 mg/g, and it was 28.73 mg/g toward Pb (II) in an aqueous solution.These results show that GMis a potential source of cellulose, which might have useful applications.
Kinematic and Thermodynamic Structures of Mesoscale Convective Systems During Heavy Rainfall in Greater Jakarta Nuryanto, Danang Eko; Pawitan, Hidayat; Hidayat, Rahmat; Aldrian, Edvin
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

A mesoscale convective system (MCS) is a large complex convective cloud system associated with a contiguous rainfall area that contributes significantly to heavy rainfall. This study analyzed the kinematic and thermodynamic structures of MCS during a heavy rainfall event. The MCSs that coincided with the heavy rainfall event and covered GJ occurred on January 17, 2013, 2014, and February 9, 2015. The three MCS cases were described from satellite observations over GJ during heavy rainfall. The main data consisted of satellite cloud top temperatures and national weather service soundings. We found a cloud shield with a temperature ≤ 221 K size and size less than 30,000 km2 at the mature stage of the MCS. Low moisture convection was unstable prior to MCS development. The warm moist air at 500–400 hPa could contribute to heavy rainfall above GJ. We suspect that the strong low-level convergence winds pro-duced an updraft, and high moist air led to a developing convective cloud. Themoist atmosphere on the third MCS was not always higher than others, but wind was low. These conditions caused the high intensity of heavy rainfall that oc-curred in GJ on the third MCS.
Molecular Dynamics Simulations of Iron-Joining Using Copper as a Filler Metal Munaji, Munaji; Buntoro, Ghulam Asrofi; Purniawan, Agung; Arifin, Rizal
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

The study of theliquid filler metal infiltration on the narrow channel of adjoining metal bears importance in understanding the mechanism of the metal brazing process. In this study, we employed the molecular dynamics simulation to understand the mechanism of Cu liquid infiltration through the narrow channel of Fe slabs. Our simulation showed that the wetting process of Fe surfaces by Cu liquid precedes the infiltration process. This study also revealed that the channel became narrower and blockages were found in the channel due to the deformation of Fe surface. In addition to the effect of viscous drag, this process should also contribute to the decreasing speed of the Cu liquid front.
Development of an Environment-Friendly and Solvent-Free Synthetic Route for the Synthesis of 3,4-Dihydropyrimidin-2-(1H)-Ones/Thiones Using La(NO3)3.6H2O as an Efficient Catalyst Mohamadpour, Farzaneh
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

We present a facile and environmentally friendly procedure for the synthesis of corresponding 3,4-dihydropyrimidin-2-(1H)-ones/thiones derivatives. The synthesis was achieved using aone-pot three-component Biginelli reaction among β-keto esters (methyl or ethyl acetoacetate), aromatic aldehyde (benzaldehyde derivatives), and urea or thiourea in the presence of lanthanum (III) nitrate hexahydrate (La(NO3)3.6H2O), as a highly efficient catalyst under solvent-free conditions. This protocol has numerous advantages: it isan inexpensive, non-toxic, simple reaction work-upcatalyst with a high atom-economy, and shows excellent yields with short reaction times.
Construction of pcDNA3.1 Vector Encoding RpfD Gene of Mycobacterium tuberculosis Rakhmawati, Aprilia; Rukmana, Andriansjah; Karuniawati, Anis
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

Tuberculosis (TB) is an infectious diseasecaused by Mycobacterium tuberculosis (M. tuberculosis). TB is still a major health problem. The Bacillus Calmette-Guérin (BCG) vaccineis the only one available for TB and is known to confer variable levels of protection. Because of thisvariability, a new vaccine is needed to control TB. Proteins secreted by M.tuberculosisare known to induce protective immunity. Within the genome of M. tuberculosis, there is a family of proteins called resuscitation promoting factor (Rpf), which playsa role in the reactivation of M. tuberculosis. RpfD is amember of the Rpf family that has been shown to be immunogenic, makingitsuitable for use as a TB vaccine. The rpfD gene of the M. tuberculosis Beijing strain from the bacterial stock of the Department of Microbiologyat the Medical Facultyof theUniversitas Indonesia was amplified using polymerase chain reaction (PCR) and then insertedintothemammalian expression vector pcDNA3.1(+). Then, the pcDNA3.1(+)-rpfD vector was transformed to Escherichia coli DH5α. A 465-bp target fragment was obtained, and the accuracy ofthecloning was confirmed using colony PCR, restriction enzyme digestion, and sequencing. We expect that this recombinant plasmid will induce immunity in future animal models and thus will prove itself to be a candidate for an M. tuberculosis vaccine.

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