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All Journal Jurnal Teknologi Dan Industri Pangan Jurnal Sain Veteriner Jurnal Ilmu Ternak JURNAL ILMU DAN TEKNOLOGI PETERNAKAN Dharmakarya : Jurnal Aplikasi Ipteks Untuk Masyarakat Majalah Kulit, Karet, dan Plastik AKSIOLOGIYA : Jurnal Pengabdian Kepada Masyarakat ANNALES BOGORIENSES Media Kontak Tani Ternak Journal of Social Research Jurnal Teknologi Hasil Peternakan Agrivet: Jurnal Ilmu-ilmu Pertanian dan Peternakan Madani: Multidisciplinary Scientific Journal Jurnal Agripet Annales Bogorienses
Wendry Setiyadi Putranto
Universitas Padjadjaran
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Journal : Annales Bogorienses

 1 
The Purification of Rennin-Like Protease from Lactobacillus paracasei Isolated from Ettawa Goat Milk Putranto, Wendry Setiyadi; Mustopa, Apon Zaenal; Kusumawati, Arizah; Prastyowati, Anika
Annales Bogorienses Vol. 24 No. 2 (2020): Annales Bogorienses
Publisher : BRIN

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There is a protease produced by bateria that has characteristics similar to rennin from a calf. Rennin has the ability to clot casein in milk. Rennin-like protease (RLP) is produced by bacteria extracellularly. Lactic Acid Bacteria (LAB) have the potential to be developed for RLP production because they are safe and non-pathogenic bacteria. Rennin is needed in the process of milk coagulation to subsequently obtain a curd in the process of making cheese. In this study, the LAB isolated from Ettawa goat milk (isolate 2.12) which produced RLP was 99% identical to Lactobacillus paracasei based on 16S rRNA gene sequence analysis. The purification of the RLP L. paracasei 2.12 with 60% ammonium sulfate deposition, dialysis, and filtration gel chromatography Sephadex G-50 showed a single 38 kDa protein band with SMCA/SPA was 4.48 higher than that of the calf rennet with a ratio value of 1, therefore in this study, RLP L. paracasei 2.12 was developed as an alternative to renin in cheese making.
Partial Purification, Characterization, and Application of Extracellular Aspartic Protease from Lactobacillus casei WSP in Producing the Bioactive Peptides with Antibacterial and Antioxidant Activity Solikhin, Akhmad; Mustopa, Apon Zaenal; Suharsono, Suharsono; Putranto, Wendry Setiyadi
Annales Bogorienses Vol. 22 No. 2 (2018): Annales Bogorienses
Publisher : BRIN

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Lactobacillus casei WSP-derived an aspartic protease was sequentially purified by using chromatography gel filtration sephadex G-50. It resulted in a 22.81-fold increase of specific activity (51.5 U/mg) with a final yield of 1.9%. The estimated molecular weight of the purified enzyme was 37 kDa and showed gelatinolytic activity in zymogram assay. The enzyme exhibited optimum activity at 40ºC and pH 6 with casein as the substrate. Enzyme activity was significantly inhibited by pepstatin A (0.5 mM and 1 mM), confirming that this enzyme is a group of aspartic proteases, while other inhibitors such as EDTA, PMSF and iodoacetic acid showed no inhibition effect on the activity of enzyme. The addition of metal ion to the enzyme decreased enzyme activity, indicating the proteolytic enzyme was metal ion- dependent. Denaturant such as DDT tended to increase caseinolytic activity. Furthermore, this enzyme was capable of generating the new peptides from skimmed milk with the size 8 kDa, 10 kDa and 15 kDa. These peptides have potential as antibacterial and antioxidant agents.
Enterococcus faecium 1.15 Isolated from Bakasam Showed Milk Clotting Activity Putranto, Wendry Setiyadi; Suradi, Kusmajadi; Chairunnisa, Hartati; Mustopa, Apon Zaenal; Kusumaningrum, Harsi Dewantari; Suhartono, Maggy Thenawidjaja
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : BRIN

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Rennin-like protease of many microorganisms behave similarly to chymosin and are potential alternatives of rennet. The lactic acid bacteria with milk clotting activity were isolated from Bakasam, an Indonesian traditional fermented meat. Screening assay was carried out using modified method of skim milk agar and milk clotting activity test, and the isolate was then identified using 16S rRNA. We found 4 isolates that showed MCA of 18-20 SU/mL. Identification using 16S rRNA indicated that the isolate ALG.1.15 was 99% identical with Enterococcus faecium. The isolate potentially produced renin-like protease to subtitute renin from veal.
Co-Authors Afifa Kantamaryana, Fatia Nasyna Akhmad Solikhin Akhmad Solikhin Aliifah, Felicia Altasya Frilanda Andry Pratama Andry Pratama Andry Pratama, Andry Anika Prastyowati Anika Prastyowati, Anika Apon Zaenal Mustopa Apon Zaenal Mustopa Apon Zaenal Mustopa Apon Zaenal Mustopa Arizah Kusumawati Azzahro, Faiz Muzaki Badruzzaman, Deden Zamzam Bambang Kholiq Mutaqin Deden Zamzam Badruzzaman Dewi, Resa Rosliana EKA WULANDARI Eka Wulandari Eka Wulandari Eka Wulandari Fajar Firdaus Afandi Fatmah Nur Anggraini Harsi D. Kusumaningrum Hartati Chairunnisa Hartati Chairunnisa Husmy Yurmiati I Made Joni I Wayan T. Wibawan Ida Ayu Marintan Raisanti Iin Susilawati In-In Hanidah Indira Lanti Kayaputri Iwan Setiawan Jajang Gumilar Kusmajadi Suradi Kusmajadi Suradi Kusmajadi Suradi Kusmajadi Suradi Kusumawati, Arizah Larasati, Alfanny Hasna Putri Lathifa, Aghisna Dwi Lilis Suryaningsih Lilis Suryaningsih Lilis Suryaningsih Lilis Suryaningsih Lizah Khairani MAGGY T. SUHARTONO Maggy Thenawidjaja Suhartono Manasje Manoah Bani Maulana, Alwi Rizal Mia Miranti Rustama Muhamad Raihan Aufa Nina Mardiana (F01108057) Obin Rachmawan Pratiwi, Fadila Rahma Dinda Puspo Edi Giriwono Putri, Agni Annisa Putri, Cindy Meylia Raden Febrianto Christi Roostita L Balia Sahbani, Lathifah Nur Saleh, Muhammad Rhafly Soerya, Fatima Aulia Sri Budiarti Poerwanto Stefanus Jemianus Lepa Suharsono Suharsono Suharsono Suharsono Trianingtyas Kusuma Anggaini Utama, Dicky Tri Waskita, Pranyata Tangguh Yuliastri, Desi Yustisia, Eva Sanum Zainatul Hayati