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All Journal HAYATI Journal of Biosciences Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences Animal Agricultural Journal Jurnal Biosains Pascasarjana Indonesian Journal of Tropical and Infectious Disease UNEJ e-Proceeding Orbith : Majalah Ilmiah Pengembangan Rekayasa dan Sosial BERITA BIOLOGI Jurnal Kimia Riset AGRISAINTIFIKA Jurnal Ilmu-ilmu Pertanian Indonesian Journal of Chemistry CHEESA: Chemical Engineering Research Articles Molekul: Jurnal Ilmiah Kimia ALKIMIA : Jurnal Ilmu Kimia dan Terapan Jurnal Abdi: Media Pengabdian Kepada Masyarakat Bubungan Tinggi: Jurnal Pengabdian Masyarakat Jurnal Layanan Masyarakat (Journal of Public Service) Berkala Penelitian Hayati Tadbiruna: Jurnal Manajemen Pendidikan Islam Molekul: Jurnal Ilmiah Kimia

Sri Sumarsih

Chemistry Department, Faculty Of Sciences And Technology Airlangga University

Author-ID : 392094

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

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Exploration of Lipase Enzyme from Soil through Metagenomic Approach Sri Sumarsih; Afaf Baktir; Budi Putri Ayu Andina
UNEJ e-Proceeding Indonesian Protein Society (IPS), International Seminar and Workshop 2014
Publisher : UPT Penerbitan Universitas Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar

This research aimed to explore lipase enzyme from soil through metagenomic approach. The DNA was extracted directly from the topsoil and river sediment by SDS-based lysis method. The soil genomic DNA was sheared into approximately 40-kb fragments The construction of genomic library was carried out by cloning the fragment DNA into fosmid pCC2FOS vector and host E. coli EPI300-T1R accordance with the protocols of CopyControl™ Fosmid production library kit. Screening of lipase-producing clones was performed based on its lipolytic activity using Luria-Bertani agar plate 12.5 µg/ ml chloramphenicol, 10 µg/ml Rhodamine B and 1 % olive oil as a substrate. The assay plates were incubated at 550 C. The lipolytic activity was identified as an orange around colonies. There were 5 (five) clones of 32 screened-clones that expressed lipolytic activity. The next research will characterize the enzyme and determine the sequence of the enzyme-encoding gene. Keywords: Lipase, soil, metagenomic, fosmid vector, pCC2FOS, E. coli EPI300-T1R

KINERJA Saccharomyces cerevisiae REKOMBINAN [GLO1] DALAM PROSES SIMULTAN HIDROLISIS PATI DAN FERMENTASI UNTUK PRODUKSI BIOETANOL Afaf Baktir; Nur Cholifah; Sri Sumarsih
BERITA BIOLOGI Vol 9, No 5 (2009)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v9i5.1983

Recent development in fermentations for bioethanol production were focused three factors, i.e. abundance and cheap substrates,superior yeast fermenting the substrates, and simultaneous saccharification and fermentation (SSF) technology.Nowadays national and world bioethanol production still depend on sugar cane and starchy materials.This research aims to determinate the optimum simultaneous saccharification and fermentation (SSF) conditions to identify the performance of local strain Saccharomyces cerevisiae recombinant [GLO1] in the producing bioethanol from starch.The optimum conditions for SSF process are in a media composition containing glucose 2% (w/v), starch 5% and at aeration rate 50 rpm.At these optimum conditions Saccharomyces cerevisiae recombinant [GLO1] produce 25.36% (v/v) bioethanol at day-20 of the fermentation process design.

EKSPLORASI GEN ENZIM LIPASE PADA TANAH PENGOLAHAN LIMBAH KELAPA SAWIT DENGAN PENDEKATAN METAGENOMIK Sri Sumarsih; Andre Pratama; Afaf Baktir
Jurnal Kimia Riset Vol. 2 No. 1 (2017): Juni
Publisher : Universitas Airlangga, Campus C Mulyorejo, Surabaya, Indonesia

Abstrak Enzim lipase merupakan bagian dari enzim hidrolase yang bekerja pada ikatan ester. Enzim ini juga mengkatalisis beberapa jenis reaksi sehingga merupakan enzim yang potensial diaplikasikan ke berbagai bidang seperti industri tekstil, kulit, deterjen, makanan, dan lain-lain. Salah satu cara mendapatkan enzim novel ialah dengan pendekatan secara metagenomik dari sampel lingkungan tanpa melalui kultur di dalam laboratorium. Sampel lingkungan yang biasa diteliti ialah memiliki keadaan ekstrem atau memiliki sumber substrat enzim yang ingin dieksplorasi. Pada penelitian ini dilakukan eksplorasi gen enzim lipase pada tanah hasil pengolahan limbah kelapa sawit (POME) melalui pendekatan metagenomik menggunakan desain primer degenerate untuk gen enzim lipase untuk golongan HSL. Didapatkan fragmen gen lipase yang memiliki ukuran 250-300 pasang basa dan dilakukan kloning ke dalam plasmid pET-30a(+) dengan sel inang E. coli TOP10 menghasilkan pustaka fragmen lipase limbah sawit (PFL2S) sebanyak 26 klon. Kata kunci: Lipase, metagenomik, primer degenerate

SINTESIS, KARAKTERISASI DAN UJI AKTIVITAS SENYAWA KOMPLEKS Zn(II)-KATEKIN SEBAGAI INHIBITOR ENZIM LIPASE Antyka Lutfiana Putri; Sri Sumarsih; Harsasi Setyawati
Jurnal Kimia Riset Vol. 4 No. 1 (2019): Juni
Publisher : Universitas Airlangga

ABSTRACT The study aims to synthesis, characterization and activity testing of Zn(II)-catechin as lipase inhibitor activity. The complex compound from synthesis result is characterized by its maximum wavelength, functional groups, metals and ligands bonds, and it’s melting point. This complex compound tested of Zn(II)-catechin as lipase inhibitor activity to p-NPP (para-nitrofenilpalmitat) substrate. The result shows that Zn(II)-catechin could be synthesized from Zn(II) ligans and metals with ratio ligands and metals mol is 1:1, that has maximum wavelength 454 nm, which contain Zn-O bond at 354,90 and 478,35 cm-1, and melting point of Zn(II)-catechin >250 oC. Zn(II)-catechin can inhibition 60,63% from concentration 50 µg/mL with mixed inhibition Keyword : Zn(II)-catechin, lipase, mixed inhibition ABSTRAK Penelitian ini bertujuan untuk melakukan sintesis, karakterisasi dan uji aktivitas senyawa kompleks Zn(II)-katekin terhadap aktivitas inhibitor enzim lipase. Senyawa kompleks hasil sintesis dikarakterisasi panjang gelombang maksimumnya, gugus fungsi serta ikatan logam dan ligannya, serta titik lelehnya. Senyawa kompleks diuji aktivitas inhibitor enzim lipase terhadap substrat p-NPP (paranitrofenilpalmitat). Hasil penelitian menunjukkan bahwa senyawa kompleks Zn(II)-katekin dapat disintesis dari ligan katekin dan logam Zn(II) dengan perbandingan mol ligan logam 1:1, mempunyai panjang gelombang maksimum 454 nm, mengandung ikatan Zn-O pada 354,90 dan 478,35 cm-1 dan titik leleh senyawa kompleks >250 oC. Senyawa kompleks Zn(II)-katekin pada konsentrasi 50µg/mL mempunyai daya inhinbisi sebesar 60,63% terhadap enzim lipase dengan jenis inhibisi campuran. Kata kunci : Zn(II)-katekin, lipase, inhibitor campuran

Komposit Kolagen Fibril-Alginat Sebagai Kandidat Membran Hidrogel Skin Substitute Faiq Nadiatul Mardia Asa; Sri Sumarsih; Andi Hamim Zaidan
Jurnal Biosains Pascasarjana Vol. 18 No. 2 (2016): JURNAL BIOSAINS PASCASARJANA
Publisher : Universitas Airlangga

AbstrakTelah dilakukan sintesis membran hidrogel komposit berbahan kolagen, alginat sebagai kandidat skin substitute. Tujuan dari penelitian ini adalah untuk mengetahui sifat fisikokimia dari membran hidrogel komposit kolagen-alginat. Metode yang dilakukan yaitu dengan teknik kering udarakan yang dicetak pada mika tipis selama tujuh hari pada suhu ruang. Hasil sintesis dikarakterisasi dengan PSA untuk mengetahui distribus ukuran nanopartikel perak, FTIR, penentuan morfologi dengan SEM, uji absorbsi dengan larutan PBS (Phospate Buffer Saline) uji kuat tarik, uji elongasi, uji sitotoksisitas dan uji antibakteri. Hasil analisis FT-IR pada membran memperlihatkan serapan kolagen dan alginat yang ditunjukkan dengan munculnya pergeseran pita serapan pada membrane komposit yaitu adanya Amida I dari kolagen, gugus karbonil (C=O) dari alginat. Hasil pengujian SEM membran komposit tanpa nanopartikel perak menunjukkan penebalan dinding dan pori yang lebar, sedangkan membran dengan penambahan nanopartikel perak ukuran pori lebih kecil. Berdasarkan hasil pengujian absorbsi menunjukkan semakin banyak komposisi kolagen pada membran maka semakin menurun lama membran hidrogel komposit menyerap larutan. Hasil pengujian kuat tarik menunjukkan nahwa semakin banyak komposisi kolagen pada membran hidrogel komposit maka semakin tinggi nilai kuat tariknya. Hasil uji elongasi menunjukkan semakin banyak komposisi kolagen maka semakin menurun nilai elongasinya.Kata kunci : membran hidrogel, kolagen, alginat

The potency of Micrococcus sp. L II 61 bacteria as oil sludge cleaning agent Ni’matuzahroh Ni’matuzahroh; Intan Ayu Pratiwi; Tini Surtiningsih; Fatimah Fatimah; Sri Sumarsih
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 22 No 2 (2017): June 2017
Publisher : The East Java Biological Society

This research aimed to reveal the ability of Micrococcus sp. L II 61 bacteria that was isolated from Pegirian Surabaya as oil cleaning agent. This is an experimental research to detect the presence of biosurfactant and lipase enzyme in culture supernatant of Micrococcus sp. L II 61 with aliphatic hy-drocarbon (cooking oil) as a substrate growth. Biosurfactant production was evaluated by measuring the surface tension of supernatant using tensiom-eter du Nouy and measuring the emulsification activity value using diesel oil as hydrocarbon test. Lipase enzyme was detected by measuring lipolitic activity value of crude enzyme (culture supernatant) by using p-nitrofenil palmitic (p-npp) as a substrate test. Data were analyzed descriptively. The results showed that Micrococcus sp. L II 61 produced biosurfactant with surface tension decreasing of culture supernatant up to 30.27 ± 1.17 mN/m compared than aquadest and value of hydrocarbon emulsification activity (AE 1 hour) up to 20.24 ± 0.68 %. Culture of Micrococcus sp. L II 61 after 16 hours incubation have a lipolytic activity 33.53 ± 0.14 U/mL at pH 7 and 37 oC. Supernatant of Micrococcus sp. L II 61 100% (v/v) give the high-est percentage of oil sludge solubility, i.e. 86.38 ± 2.39%. Micrococcus sp. L II 61 is a highly potential to be developed as oil sludge cleaning agent.

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%.

HIDROLISIS BEBERAPA JENIS XILAN DENGAN ENZIM XILANOLITIK TERMOFILIK REKOMBINAN Ni Nyoman Tri Puspaningsih; Hery Suwito; Sri Sumarsih; Ali Rohman; One Asmarani
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 12 No 2 (2007): June 2007
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/353

The aims of this research were to know the ability of recombinant xylanolytic enzyme from recombinant E. coli DH5a (pTP510) to hydrolyze several commercial xylan and analysis the reduction sugar product. Recombinant xylanolytic enzyme (exo-xylanase, b-xylosidase and a-L-arabinofuranosidase) could hydrolyzed several commercial xylan (oat-spelt xylan, birchwood, wheat, rye, and arabinan) with xylanolytic activities are: oat-spelt xylan (1.73 U/mL), birchwood (0.92 U/mL), wheat (6.52 U/mL), rye (4.94 U/mL), and arabinan (3.40 U/mL). Xylanolytic enzyme assay use specific substrate p-nitrophenyl-b-D-xylopyranoside (pNP-X) shown xylosidase activity 15.869 U/mL. Hydrolysis product was analyzed by HPLC. The results showed that xylose, arabinose, and xylo-oligosaccharide were produced from birchwood, wheat, rye, and arabinan hydrolysis, although xylose and arabinose were produced from hydrolysis of oat-spelt xylan.

EKSPRESI GEN PENYANDI b-XILOSIDASE DALAM SISTEM pHIS1525/ Bacillus megaterium MS941 Sri Sumarsih; Ni Nyoman Tri Puspaningsih; Sofijan Hadi; Ami Soewandi J.S.
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 13 No 2 (2008): June 2008
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/364

The aim of this research was to express the β-xylosidase gene in the pHIS1525/ Bacillus megaterium MS941 system. The xyl gene was amplified from pTP510 and cloned into pHIS1525 in E. coli DH10β. The recombinant plasmid was transformed into B. megaterium MS941 by protoplast transformation. Transformants were selected by growing the recombinant B. megaterium MS941 on solid LB medium containing tetracycline (10 μg/ ml). The expression of β-xylosidase was assayed using 0.2% methylumbelliferyl-β-D-xyloside (MUX) and the proteins were analyzed by SDS-PAGE method. The β-xilosidase activity was determined toward p-nitrophenyl-β-Dxylopyranoside (pNPX) as a substrate and p-nitrofenol releasing was measured by UV/Vis spectrophotometer at λ = 405 nm. This research showed that recombinant B. megaterium MS941 expressed the β-xylosidase gene (xyl) and secreted it into the culture medium. The SDS-PAGE analysis of extracellular protein (culture medium) showed a 60,0 kD protein band. The recombinant Bacillus megaterium MS941 expressed and secreted the β-xilosidase into culture medium 5 hours after adding 5% xylose. The b-xylosidase activity was 0.441 unit/ml toward pNPX as a substrate.

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 A. Budi Prasetyo A.A. Ketut Agung Cahyawan W Abdulloh Abdulloh AFAF BAKTIR Ahlan Riwahyu Habibi Ahmadi Jaya Permana Alfa Akustia Widati Ali Rohman Ami Soewandi J.S. Andi Hamim Zaidan Aning Purwaningsih Antyka Lutfiana Putri Aryati Aryati Ati, Nur Ing Atik Widiyanti Aulianitha Salsabella B. Sulistiyanto Badi’atul Azizah Bambang Piluharto Bambang Sulistiyanto Budi Prasetyo, Antonius Budi Putri Ayu Andina Budi Putri Ayu Andina, Budi Putri Ayu C.I. Sutrisno Cahya Setya Utama Cornelius Imam Sutrisno Dwi Kusuma Wahyuni Dwi Sunarti Edjeng Suprijatna Faiq Nadiatul Mardia Asa Fajrina, Ishmah Tri Faozi, Ahmad Aziz Fatiha Khairunnisa Fatimah Fatimah Fatimah Ganden Supriyanto Gilva Illavi Hamami Handoko Darmokoesoemo Hanny Indrat Wahyuni Harini Nur Hikmah Harsasi Setyawati Hartati Hartati Hartati Hartati Haryanto, Darban Hera Lisna Ginawati Hery Suwito Hwei Voon, Lee Ilham Harlan Amarullah Intan Ayu Pratiwi, Intan Ayu Kariza Makanty Kautsar Ul Haq Kris Cahyo Mulyatno, Kris Cahyo Luthfi Djauhari Mahfudz Masanori Kameoka, Masanori Maylina Ilhami Khurniyati Ma’rifah, Binti Mei Shirli Yasinta Miratul Khasanah Mochamad Zakki Fahmi Mochammad Imron Awalludin Muji Harsini Mulyadi Tanjung Ni Nyoman Tri Puspaningsih Nira Ambar Arum Ni’matuzahroh Ni’matuzahroh Novia Fajarwati, Novia NUR CHOLIFAH Nur Cholifah One Asmarani Purkan Purkan Purkan Purkan, Purkan Purwaningsih, Aning Qurrota A’yuni Rahayu, E.S Rico Ramadhan, Rico Rike Cahyo Probowati Rina Muryani Rizka Diah Fitri Sarjana, Teysar Adi Sevia Ayuningtyas Shihah, Hanna Dzawish Siti Churrotin, Siti Siti Wafiroh Soegeng Soegijanto Sofijan Hadi Solly Aryza Sri Kismiati, Sri Sri Mukodiningsih Sri Subekti Sulistiyanto, B Tampoebolon, B. I. M. Teguh Hari Sucipto, Teguh Hari Tini Surtiningsih Tokok Adiarto Tokok Ardiarto Tomohiro Kotaki, Tomohiro Ueda, Shuhai Uswatun Chasanah Virgawati, Sari Wahyuni, Nur Maulida Wardhani, Puspa Wulandari, Melysa Yanuardi Raharjo, Yanuardi

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