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All Journal HAYATI Journal of Biosciences MEDIA PETERNAKAN - Journal of Animal Science and Technology Jurnal Ilmu Pertanian Indonesia Jurnal Teknologi Dan Industri Pangan Jurnal Akuakultur Indonesia Microbiology Indonesia BIOTROPIA - The Southeast Asian Journal of Tropical Biology Journal of Tropical Soils BERKALA SAINSTEK Biota: Jurnal Ilmiah Ilmu-Ilmu Hayati Jurnal Penelitian Pascapanen Pertanian Indonesian Journal of Biotechnology Jurnal Sumberdaya Hayati BERITA BIOLOGI JURNAL BIOLOGI INDONESIA Jurnal Bioteknologi & Biosains Indonesia (JBBI) JFMR (Journal of Fisheries and Marine Research) Jurnal Penelitian Pendidikan IPA (JPPIPA) Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology BIOEDUSCIENCE Jurnal Ilmu Nutrisi dan Teknologi Pakan ANNALES BOGORIENSES Biosaintifika: Journal of Biology & Biology Education Menara Perkebunan Makara Journal of Science Jurnal Natural Annales Bogorienses Berita Biologi

Anja Meryandini

Biology Department, Faculty Of Mathematics And Natural Sciences, IPB University And Biotechnology Center, Bogor 16680, Indonesia

Author-ID : 229368

Agriculture, Biological Sciences & Forestry Astronomy Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Education Energy Engineering Environmental Science Immunology & microbiology Industrial & Manufacturing Engineering Materials Science & Nanotechnology Mathematics Medicine & Pharmacology Neuroscience Physics Veterinary

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Screening of Proteolytic Enzymes of Streptomyces sp. Local Strain and Their Characterization DERI YURATMOKO; NISA RACHMANIA MUBARIK; ANJA MERYANDINI
Microbiology Indonesia Vol. 1 No. 2 (2007): August 2007
Publisher : Indonesian Society for microbiology

Protease of two Streptomyces sp. strain were chosen for characterization because of the large clear zone surrounding the colony in nutrient agar media containing 1% (w/v) skim milk. Extracellular protease from the two isolates SLW 8-1 and 45I-3 were characterized following incubation of the isolate in Nutrient Broth media containing skim milk or chicken feather (1%). The optimum activity of the protease SLW 8-1 was at pH 9 and 80 ºC, whereas that of the keratinase was at pH 6.5 and 70 +C. Protease of strain 45I-3 showed its optimum activity at pH 7.5 and 50 ºC whereas the keratinase was at pH 8.5 and 80 ºC.

Activity of Proteolytic and Amylolytic Enzymes from Bacillus spp. Isolated from Shrimp Ponds IT JAMILAH; ANJA MERYANDINI; IMAN RUSMANA; ANTONIUS SUWANTO; NISA RACHMANIA MUBARIK
Microbiology Indonesia Vol. 3 No. 2 (2009): August 2009
Publisher : Indonesian Society for microbiology

Accumulation of feed excess in commercial shrimp ponds due to overfeeding could decrease water quality. Protein and starch are the primary components of shrimp feed. This study was conducted to characterize extracellular proteases and amylases of Bacillus spp. isolated from shrimp ponds. 72 proteolytic and amylolytic Bacillus spp. isolates were screened from shrimp ponds in Karawang, West Java. Ten isolates were selected for further characterization for their growth and ability to reduce total suspended solid generated from commercial shrimp feed. Bacillus sp. DA 5.2.3 and L5 showed excellent activity in reducing total suspended solid, by 37 and 30% respectively. Protease and a-amylase activities of Bacillus sp. DA 5.2.3 isolate were consistently higher than that of L5. Maximum total and specific protease activity of DA 5.2.3 isolate was 2.0 U mL-1 and 40.9 U mg-1 respectively, while the activities of the L5 isolate were 2.1 U mL-1 and 23.0 U mg-1 respectively. Based on its 16S rRNA gene sequences, Bacillus sp. DA 5.2.3 showed 99% similarity to Bacillus cereus XHJ-2-6. Bacillus sp. DA 5.2.3 could potentially be applied to maintain water quality by reducing total suspended solid in water columns of shrimp ponds.

Optimization of Xylanase Production by Streptomyces costaricanus 45I-3 Using Various Substrates through Submerged Fermentation SIPRIYADI SIPRIYADI; ARIS TRI WAHYUDI; MAGGY THENAWIDJAYA SUHARTONO; ANJA MERYANDINI
Microbiology Indonesia Vol. 14 No. 1 (2020): March 2020
Publisher : Indonesian Society for microbiology

Xylanase is an important hydrolytic enzymes with many application in several industries, but to obtain enzyme derived products is not easy. Thus, the optimization of efficient xylanases production is a great interest for biotechnological application. This study aims to determine the type of substrate, medium composition, and optimum conditions of xylanase production by S. costaricanus 45I-3. Determination of substrate type was done by growing the tested bacteria on birchwood xylan, beechwood xylan, oat spelled xylan, corn cobs xylan, and tobacco xylan substrate, meanwhile the determination of medium composition and enzyme production were done by measuring xylanase activity at various substrate concentration and replacing the carbon, nitrogen, phosphate and surfactants source. The results showed that the highest enzymatic index (EI) produced from corn cob xylan substrate at 3.60 meanwhile the second highest was beechwood xylan substrate at 2.87 EI, however this substrate is purer, thus this substrate was selected and used as xylan sources for further optimization measurement. The best xylanase activity (2.29 U/mL) obtained on eighth day after inoculation on rotary incubator at 120 rpm in 28 ÂºC. Arabinose as the source of carbon generate the highest activity at 3.161 U/mL meanwhile the most preferred source of phosphate is Na2HPO4 (2.37 U/mL). Both source of nitrogen i.e. nitrogen ammonium sulphate (NH4)2SO4 and yeast extract were able to produce xylanase at 2.57 and 2.36 U/mL. The addition of surfactant in production medium showed addition of SDS surfactant (0.146 U/mL) and Tween 80 (0.438 U/mL) showed a negative response by decreasing the activity. The conclusion showed that the xylanase activity was increased after optimization at various C, N, and P sources, and the use of nitrogen source (NH4)2SO4), become a more economical alternative to replacing a nitrogen source yeast extract so it can lower the production costs of xylanase enzyme.

The ethanol Production Activity of Indigenous Thermotolerant Yeast Pichia kudriavzevii 1P4 DAROJATUL ULYA; RIKA INDRI ASTUTI; ANJA MERYANDINI
Microbiology Indonesia Vol. 14 No. 4 (2020): December 2020
Publisher : Indonesian Society for microbiology

Pichia kudriavzevii 1P4 is a thermotolerant-ethanologenic yeast potential for application in ethanol industry. In this study we evaluated the stress tolerance phenotype of P. kudriavzevii 1P4 in dealing with fermentation related-stresses, including high temperature stress, high sugar content, ethanol content and the fermentation capacity of the particular isolate. Based on spot assay, 1P4 showed stress tolerance phenotype against high sugar concentration for up to 30% sugar content and 10% ethanol stress. In addition, 1P4 was capable to show temperature-stress tolerance phenotype for up to 42oC, suggesting that 1P4 belong to thermotolerant yeast isolate. Fermentative activity was measured by using glucose consumption and ethanol production assay. We evaluated the fermentative and growth rate of 1P4 at various temperature condition which were 27oC, 37oC and 42oC using YPD media (at initial glucose of 2%, 10% and 20%). Interestingly, 1P4 consumed the highest glucose in 20% of concentration at 37oC (15.29%), simultaneously with the highest concentration of ethanol (32.05 g/L ethanol and 0.67 g/L/h ethanol productivity). Cell growth analysis showed that growth of 1P4 isolate increased with higher initial glucose condition yet decreased as temperature during fermentation was raised. The growth rate of 1P4 was found high in 20% initial glucose at 37oC than 2% and 10% at same temperature. In addition, 1P4 exhibited short lag phase at high-temperature fermentation. Our data indicate that 1P4 can potentially be applied as fermentation agent especially in high-temperature ethanol fermentation. Key words: bioethanol production, fermentation related-stress, thermotolerant yeast

Co-Authors . Hamim . KURRATAA’YUN . YOPI . YOPI ., Yopi ., Yopi A, Gading Wilda A, Gading Wilda Abd. Rasyid Syamsuri Abdjad Asih Nawangsih Adawiah, Adilah Ade Andriani ADE ANDRIANI Ade Irma Ahmad Thontowi Aisyah, Nadira Alfred Michael ALINA AKHDIYA Amor Tresna Karyawati, Amor Tresna Andika Susantri Anggreandari, Rizky Antonius Suwanto Apon Zaenal Mustopa Ardana Kurniaji Ariandi Arina Amalia Putri Aris Tri Wahyudi Ariyanto, Yogy Satria Armita, Dea Asrianti Basri Atit Kanti Azizah Hikma Safitri Azizah, Malikah Bambang Prasetya Basri, Asrianti Basri, Asrianti Bedah Rupaedah Berutu, Cocok Ana Maryani Berutu, Cocok Ana Maryani Besty Maranatha Birahy, Deford Cristy Candra Sunarti , Titi Cocok Ana Maryani Berutu Cynthia Rizka Riani DAROJATUL ULYA Deden Saprudin DERI YURATMOKO DEWI APRI ASTUTI Dewi, Fitria DIMAS ANDRIANTO DINI NURDIANI Dwi Ambarawati Dyah Iswantini EKA RURIANI Elly Rosyidah Engelhaupt, Martin Esti Utarti Fahrurrozi Fahrurrozi Fahrurrozi Fahrurrozi Fahrurrozi Fahrurrozi Fathiah, Muhammad Fadhil Fathin Hamida Ferry Mutia Fitria Dewi Glisina Dwinoor Rembulan Hairani, Atikah Hamim Hamim Hamtini - Hamtini Hanni Tsaaqifah Hari Eko Irianto Hartono, Faisal Diniamal Hasrul Satria Hasrul Satria Nur Hasrul Satria, Hasrul I Komang Gede Wiryawan Ifah Munifah Iman Rusmana Inayah, Mazidah Noer IRA ERDIANDINI, IRA It Jamilah LAKSMI AMBARSARI Lenni Fitri Lenni Fitri Lilis Nuraida Lily Nathalia Loli Natalia Lukman, Zulfiqar Maggy T Suhartono Maggy Thenawidjaja Suhartono Maggy Thenawidjaya Suhartono Mahsunah, Anis Herliyati Manguntungi, Baso Maranatha, Besty Mareistia Fassah, Dilla Maria Sugiharti Marini Wijayanti Muhammad Nur Kholis, Muhammad Nur Muhammad Subhan Hamka MUNTI YUHANA MUTIA, FERY NANIK RAHMANI Nanik Rahmani Nanik Rahmani NAOMI, APRILIA Natalia, Loli Nathalia, Lily Niken Financia Gusmawati NISA RACHMANIA MUBARIK Nunuk Widhyastuti NUNUK WIDHYASTUTI Nur Richana Nur, Hasrul Satria Nurfadhilla Rahmadhani Nurhasna, Aprilia Prihandono, Prima Agung Puspitasari, Dian Japany Rahayu Wulan RAMADHAN, ZULFA AULIA Rika Indri Astuti Rizky Anggreandari Rosyidah, Elly SAFITRI NURLAELA SHANTI RATNAKOMALA Sidiq, Muhammad Raffel Sipriyadi Sitti Rahbiah Akram SOFIYANTO, M. EDY Sri Estuningsih Sri Koerniati Sri Listiyowati SUHARSONO Sumarni Nompo Sunarti, Titi Suyono, Meisy Nawang Titi Candra Sunarti TRIO HENDARWIN Turnip, Enita Romasni Umi Fatmawati Vestika Iskawati Wahidul Hijah Wahyu Afrilasari Wahyu Widosari WIDANARNI WIDANARNI Widosari, Wahyu WULAN, RAHAYU Yantyati Widyastuti Yaya Rukayadi Yopi - Yopi Yopi YOPI YOPI Yopi, YULIANA, META YULIN LESTARI Zahrani, Siti Mutia

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