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All Journal HAYATI Journal of Biosciences Jurnal Kedokteran Brawijaya PROSIDING SEMINAR KIMIA UNEJ e-Proceeding BERITA BIOLOGI Jurnal Kimia Riset Indonesian Journal of Chemistry Molekul: Jurnal Ilmiah Kimia Jurnal Abdi: Media Pengabdian Kepada Masyarakat Jurnal Layanan Masyarakat (Journal of Public Service) Berkala Penelitian Hayati

AFAF BAKTIR

Chemistry Department, Faculty Of Sciences And Technology Airlangga University

Author-ID : 240279

Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Decision Sciences, Operations Research & Management Earth & Planetary Sciences Education Environmental Science Immunology & microbiology Languange, Linguistic, Communication & Media Materials Science & Nanotechnology Medicine & Pharmacology Social Sciences Other

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PRODUKSI ENZIM KITINASE DARI Aspergillus niger MENGGUNAKAN LIMBAH CANGKANG RAJUNGAN SEBAGAI INDUSER Purkan Purkan; Afaf Baktir; Arju Rohmah Sayyidah
Jurnal Kimia Riset Vol. 1 No. 1 (2016): Juni
Publisher : Universitas Airlangga

AbstrakKitinase merupakan enzim hidrolitik yang dapat menghidrolisis kitin pada ikatan β-1,4-glikosidiknya dengan menghasilkan derivat-derivat kitin seperti oligomer kitin yang mempunyai banyak manfaat. Penelitian ini bertujuan untuk melakukan pengembangan produksi enzim kitinase dari sumber lokal yang melimpah di alamserta murah dengan melakukan optimasi substrat dalam hal ini digunakan substrat tetes tebu (molase) dan limbah cangkang rajungan untuk produksi enzim kitinase dari Aspergillus niger. Sebelumnya, dilakukan kultivasi isolat kapang Aspergillus niger dengan membuat kurva pertumbuhan menggunakan metode masa sel kering dimana dari hasil penelitian inokulasi optimal adalah 22 jam. Pada proses produksi, diperoleh waktu fermentasi optimal adalah 52 jam dengan menentukan uji aktivitasnya menggunakan metode turbidimetri. Hasil optimasi substrat menunjukkan bahwa enzim kitinase yang maksimal diperoleh pada penambahan molase 0,5% (b/v) dengan unit aktivitas enzim 0,14726 (U/mL) dan cangkang rajungan 2% (b/v) dengan unit aktivitas enzim yang dihasilkan 0,12826 (U/mL). Kitinase dari Aspergillus niger ini mempunyai pH optimal 6 dan suhu optimal 40 oC. Kata kunci: Aspergillus niger, kitinase, cangkang rajungan, molase AbstractChitinase is a hydrolytic enzyme that hydrolyzes chitin on β-1,4-glycosidic bond and thereby producing chitin derivatives such as chitin oligomers that have multiple benefits. The purpose of this research was to develop the production of chitinase enzyme from cheap and are abundant local nature sources, by optimizations substrate in this case the substrate used molasses and crab shell waste for the production of chitinase enzyme from Aspergillus niger. Previously, isolates of Aspergillus niger cultivated by creating a growth curve using dry cell mass method which from the results of research inoculation optimal are 22 hours. In the production process, obtained the optimum fermentation time is 52 hours to determine the activity test using turbidimetry method. Result of substrate optimizations indicate that chitinase enzyme maximum by addition of molasses obtained in 0.5% (w/v) with enzyme activity units 0.14726 (U/mL) and crab shells 2% (w/v) with enzyme activity units 0.12826 (U/mL). Chitinase from Aspergillus niger has a pH optimum 6 and temperature optimum 40 oC. Keywords: Aspergillus niger, chitinase, crab shells, molasses

PEMURNIAN PARSIAL DAN KRISTALISASI PAPAIN DARI GETAH Carica papaya Dwi Putri Mashfufatur Rohmah; Sofijan Hadi; Afaf Baktir
Jurnal Kimia Riset Vol. 4 No. 2 (2019): Desember
Publisher : Universitas Airlangga

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20473/jkr.v4i2.16902

AbstractThis research has done partial purification by fractionation and optimization crystallization of papain from Carica papaya latex with the addition of ammonium sulphate. The enhancement of purification factor was determined by its specific activity. The fractionation results show that papain fraction of Carica papaya can be obtained by adding 40-80% saturated ammonium sulphate, with the highest specific activity, i.e. 2,0819 U/µg and the factor purification increase of 6,27 fold than papain extract. Meanwhile, the highest total activity, i.e. 10,7780 U of papain crystals can be obtained by presipitant agent addition of ammonium sulphate in the level / concentration 80% saturated at 15 °C. Microscopycally papain crystals profile in this condition have cube and tetragonal shape.Key words: crystallization, fractionation, ammonium sulphate, papain

OPTIMALISASI KONDISI AMOBILISASI GLUKOMINASE MENGGUNAKAN PADATAN PENDUKUNG BENTONIT BENTUK ION UNTUK KONVERSI PATI MENJADI GULA Afaf Baktir; Sri Sumarsih; Hamami
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 1 No 1 (1995): June 1995
Publisher : The East Java Biological Society

Bentonit is a clay available in a lot of quantity and very chief. It can be activated to cation or anion exchanger like resin. His research was done in order to search a treatment and to get optimum condition for binding the glucoamylase to the bentonit, and to observe the ability of immobilized glucoamylase obtained in hydrolyzing amylum. It was done three ways to activate the bentonit, to obtain three kinds of bentonit, those are 'active bentonit' (adsorbs enzyme physically) and 'cation exchanger bentonit' consist B- NH4+, and B-H+ (bind enzyme ionically). The bentonit was contacted to glucoamylase in various condition to search the optimum condition (pH, concentration, temperature, and contact duration time). Immobilized glucomynase obtained was tested it's binding strengthness and the ability of hydrolyze amylum to glucose. The conclusion of this research were, (1) bentonit can be used as a supporting material for immobilizing glucomynase in the form of B-H+ cation exchanger, (2) the optimum condition of bentonit and glucomylase binding was in pH = 5.5 and at 25oC, contact duration time was 30 minutes, (3) immobilizes glucomylase column (height of 1 cm and diameter of 2.5 cm) had conversion ability at the level of 19.88%.

FRAKSINASI AMILASE DARI Endomycopsis fibuligera ITBRcc64 DENGAN METODE PRESIPITASI AMONIUM SULFAT Afaf Baktir
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 1 No 2 (1995): December 1995
Publisher : The East Java Biological Society

Endomycopsis fibuligera ITB.R.cc.64 produced high extracellular amylase activity. It showed two kinds of amylase activities, those are liquefication and saccharification. The aim of this research are to separate each kind of amylase by fractionation with ammonium sulfate and to test the specific activity of each fraction. It was done three fraction ammonium sulfate: 0-40 %, 40-60 %, and 60-80%. This fraction has the strong liquefication activity of 20.847 U/mg protein, the second fraction has the strong saccharification activity of 18.903 U.mg protein and the weak liquefication activity of 1.756 U/mg protein.

PRODUKSI, ISOLASI DAN KARAKTERISASI ENZIM DEKSTRANASE dari Arthrobacter sp. B7 Afaf Baktir; Untung Murdiyatmo
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 10 No 2 (2005): June 2005
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/439

Dextranase enzyme has been purified and characterized from Arthrobacter sp. B7. This enzyme was purified from the culture supernatant of Arthrobacter sp. B7 by procedure of native PAGE. The molecular size of the enzyme was estimated 72,5 kDa by SDS-PAGE. The N-terminal amino acid sequence of this enzyme determined using Edman degradation techniques were APVTADVGNLHT. SDS-PAGE and native-PAGE analysis revealed that the enzyme molecule consisted of one sub-unit.

ANALISIS 6 DNA REKOMBINAN DENGAN ENZIM EcoR1 Ni Nyoman Tri Puspaningsih; Akhmaloka; Afaf Baktir; Ami Soewandi J.S.; Y. Sriwulan M.
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 3 No 1 (1997): June 1997
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/490

Amylase enzyme from Endomycopsis fibuligera capable to hidrolize starch into glucose. Insertion of amylase gene from Endomycopsis fibuligera into yeast (Saccharomyces cereviceae) will be able to increase the function of yeast (S.cereviceae) to digest more cheaper substrate, like starch. Before cloning in yeast, recombinant DNA will be made and analyzed in Escherichia coli strain DH5a. The result showed that the sixth transformant consist recombinant DNA that were sensitive to tetracycline medium. Analysis by EcoR1 digestion showed that the size of insertion fragment into Ycp 50 vector are around 0.3 untill 16 kb.

KEMAMPUAN TUMBUH Ecoli DH5 KOMPETEN DALAM 'MEDIUM MINIMAL' MENGANDUNG DEKSTRAN UNTUK MENGEMBANGKAN METODE SELEKSI KLON GEN DEKSTRANASE Afaf Baktir; Kuntaman Kuntaman
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 7 No 1 (2001): December 2001
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/510

Dextranase gene cloning so far have used selection method base on halo formation around he recombinant dex colony grown on LB â€“ blue dextran agar plate. The difficulty of the cloning process is in the selection of dex positive clone. As an example, for obtaining dex gene it has been screened about 36500 colonies. The reason that it was difficult to determine Dex positive clone because dextran hydrolysis by primary recombinant E.coli cells in LB â€“ blue dextran medium was too weak. In the present research, we have designed a minimal medium contained dextran and low concentration of yeast extract to reduce difficulty and to increase accuracy and reproducibility determining of recombinant dex E.coli.In this experiment, dex positive cloned was simulated by competent E.coli grown in medium contained dextranase. The minimal medium designed consist of dextran 1% + yeast extract 0.01% +KH2PO4 0.1% + MgSO4 0.24% + NaCl 0.1% + CaCl2 0.01%. this medium have proved can distinguish between recombinant E.coli dex and other E.coli ie. The competent E.coli can grow well in this medium which was supplied by dextranase, but without dextranase this competent E.coli did not or limited grow

Histochemical Changes Liver and Kidney of Mice Exposed to Mercury and Recovery with Nanogold Titik Taufikurohmah; I Gusti Made Sanjaya; Afaf Baktir; Achmad Syahrani
Molekul Vol 11, No 1 (2016)
Publisher : Universitas Jenderal Soedirman

The background of this research is the circulation cosmetic with mercury that occur today in society. The problem of the research is that occur histochemical’s damage liver and kidney after exposure to mercury, and is that nanogold can recovery that damage. The pre-clinical study needed 24 mice (Mus muscullus) were divided into 6 groups, the control is A group, B group was exposed to mercury, Groups C, D, E and F after being exposed to mercury, than recovery by nanogold with concentration each of 5, 10, 15 and 20 ppm. Exposure was performed 1 week and 4 weeks of recovery. Necropsy of mice doing after treatment, liver and kidneys are processed into preparations by blocking with paraffin embedding method. Histochemical staining of liver and kidney tissue with Hematoxylin eosin (HE) to determine changes of cell constituent and staining Van Geyson to determine the structure of collagen constituent. Statistics Manova showed different results between treatment groups. Tissue damage, lysis cell and destruction of collagen can be observed from histochemical techniques for mercury-exposed group compared to the control group. Tissue and collagen recovery process can be observed from group C, D, E and F. The conclusion that the effects of mercury one week exposed through skin give effect to collagen tissue damage at liver and kidneys of mice. 20 ppm of Nanogold can recovery damaged cells and collagen tissue from the liver and kidneys of mice after four weeks of recovery.

A THERMOPHILIC MICROBE PRODUCING DEXTRANASE FROM HEATED SUGAR CANE Afaf Baktir; Zumrotul Koiriyah; Ali Rohman
Indonesian Journal of Chemistry Vol 5, No 3 (2005)
Publisher : Universitas Gadjah Mada

A thermophilic aerobe microorganism designated NP4, was isolated from the heated sugar cane. It grew on dextran, and produced a thermoactive extracellular dextranase. Screening and isolation was done by assay of dextranase activity semi quantitatively on solid medium containing blue dextran. It provided several colonies with different morphology exhibited decolourized zones around, on culture plates containing blue dextran 2000R. The screening resulted in isolation of one microbe which efficiently assimilate dextran as carbon source. Dextranase production from the choised strain in liquid medium was conducted at room temperature for 8 hours with shaking speed of 125 rpm. The dextranase enzyme showed optimum pH of 8 and optimum temperature of 60 oC.

Dual Function of Silver Nanoparticles as Matrix Extracell Removal and Antimicrobial Agent in Polymycrobial Biofilms Mei Shirli Yasinta; Hera Lisna Ginawati; Nira Ambar Arum; Harini Nur Hikmah; Sri Sumarsih; Mochamad Zakki Fahmi; Afaf Baktir
Indonesian Journal of Chemistry Vol 21, No 2 (2021)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijc.52355

Candida albicans often form polymicrobial biofilms along with pathogenic microbes. Silver nanoparticles (AgNPs) were well known to have strong antimicrobial activity. However, their effect on polymicrobial biofilms and the mechanism has never been reported. This study aimed to synthesize AgNPs and study their effects on polymicrobial biofilm represented by C. albicans–E. coli biofilm. Polymicrobial biofilms, formed by clinical isolates of C. albicans and E. coli, were developed from the standardized suspensions of each strain by culturing flat-bottom 96-well microtiter plates for 48 h, then treated with AgNPs. Cell viability was assessed using the tetrazolium salt reduction assay; the extent of biofilm formation was measured by crystal violet staining. AgNPs reduced the polymicrobial biofilm in two ways: by degrading the extracellular matrix and killing both C. albicans and E. coli. The results showed AgNPs is a potential new approach for developing potent anti-biofilms.

Co-Authors Akhmaloka Akhmaloka Ali Rohman Ami Soewandi J.S. Andre Pratama Aning Purwaningsih Arju Rohmah Sayyidah Badi’atul Azizah Budi Putri Ayu Andina Budi Putri Ayu Andina, Budi Putri Ayu Dwi Putri Mashfufatur Rohmah Fatiha Khairunnisa Fatiha Khairunnisa Hamami Harini Nur Hikmah Hartati Hartati Hera Lisna Ginawati I GUST MADE SANJAYA Kuntaman Kuntaman KUNTAMAN KUNTAMAN Loo Hariyanto Raharjo, Loo Hariyanto Masfufatun Masfufatun Mei Shirli Yasinta Mochamad Zakki Fahmi Muji Harsini Ni Nyoman Tri Puspaningsih Nira Ambar Arum Noer Kumala Noer Kumala NOER KUMALA Noor Cholies Zaini NUR CHOLIFAH Nur Cholifah Purkan Purkan Putu Oky Ari Tania Siti Wafiroh Sofijan Hadi Sri Sumarsih Sri Sumarsih Sri Sumarsih Syahrani, Achmad Titik Taufikurohmah Untung Murdiyatmo UNTUNG MURDIYATMO Y. Sriwulan M. Zumrotul Koiriyah

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