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All Journal HAYATI Journal of Biosciences Journal of Food and Pharmaceutical Science Indonesian Journal of Biotechnology The Indonesian Biomedical Journal Science and Technology Indonesia Jurnal Akta Jurnal Fitofarmaka Indonesia Jurnal Pro Hukum : Jurnal Penelitian Bidang Hukum Universitas Gresik JFIOnline Jurnal Ilmu Kefarmasian Indonesia Jurnal Jamu Indonesia JURNAL RECTUM: Tinjauan Yuridis Penanganan Tindak Pidana Devotion: Journal of Research and Community Service Narra J International Journal of Social Service and Research Jurnal Impresi Indonesia International Journal of Science and Society (IJSOC) Journal of Social Research Journal Of World Science MEDICINUS Journal of Law, Poliitic and Humanities The Indonesian Journal of Gastroenterology, Hepatology and Digestive Endoscopy INJURITY: Journal of Interdisciplinary Studies Eduvest - Journal of Universal Studies Journal of Social Science Influence: International Journal of Science Review Al Makki Health Informatics Journal Journal of Food and Pharmaceutical Sciences Asian Journal of Social and Humanities Indonesian Journal of Jamu
Raymond R. Tjandrawinata
Fakultas Bioteknologi, Universitas Katolik Indonesia Atma Jaya
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Journal : HAYATI Journal of Biosciences

 1 
Peptides Hydrolysate Derived from Collagen of Snakehead Murrel (Channa striata) Skin Demonstrate Anti-cholesterol and Anti-oxidant activities Sinaga, Wenny Silvia L. Br.; Ismaya, Wangsa T.; Retroningrum, Debbie S.; Tjandrawinata, Raymond R.; Suhartono, Maggy T.
HAYATI Journal of Biosciences Vol. 27 No. 2 (2020): April 2020
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (291.388 KB) | DOI: 10.4308/hjb.27.2.136

Abstract

Anti-cholesterol and anti-oxidant play a crucial role to combat cardiovascular disease (CVD), due to formation of arterial plagues from oxidation of cholesterol. In the past decades, bioactive peptides demonstrating anti-cholesterol and anti-oxidant activities have emerged as the alternative drugs. In this study, acid soluble collagen was extracted from the skin of snakehead murrel and employed to induce secretion of collagenase by Bacillus licheniformis F11.4. The collagenases secreted were in turn used to produce peptides hydrolysate and were grouped in two distinct collagenase fractions, designated as fraction D and F. Peptides hydrolysate produced by the fraction D was found to demonstrate HMG-CoA inhibitor activity comparable to pravastatin and limited anti-oxidant activity. Meanwhile, peptides hydrolysate generated using the fraction F demonstrated anti-oxidant activity comparable to BHT (2mM), vitamin C (2mM), and vitamin E (2mM), but limited HMG-CoA activity. Combination of the fraction D and F resulted in substantial HMG-CoA inhibition and anti-oxidant activities.
Food Origin Fibrinolytic Enzyme With Multiple Actions Laurentia Stephani; Raymond Rubianto Tjandrawinata; Diana Nur Afifah; Yanti Lim; Wangsa Tirta Ismaya; Maggy Thenawidjaja Suhartono
HAYATI Journal of Biosciences Vol. 24 No. 3 (2017): July 2017
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (919.422 KB) | DOI: 10.4308/hjb.24.3.124

Abstract

Many health related problems such as cardiovascular diseases are associated with the formation of excessive clot in the blood (thrombus). Approaches in cardiovascular disease treatment are preventing the formation or removing the thrombus. The present thrombolytic agents can be classified as plasminogen activators, fibrinolytic enzyme which directly degrades fibrinogen or fibrin and heparin type which act as thrombin inhibitor. Recently, microbial fibrinolytic enzymes of food origin receive more attention that leads to escalating efforts to explore traditional fermented foods as the natural sources. We have successfully isolated microorganism from Indonesian fermented soybean tofu dregs “Oncom” that secretes fibrinolytic enzyme. The microorganism identified as Stenotrophomonas sp. is unique because most of the reported fibrinolytic microorganism belongs to Bacillus sp. This isolate was found to produce extracellular fibrinolytic enzyme which could degrade fibrinogen and fibrin directly as determined by fibrinogen zymography and fibrin plate methods. More importantly, the 30-kD purified enzymes was found to demonstrate not only fibrin and fibrinogen degradation capabilities, but also acted as thrombin inhibitor as determined using specific substrates for thrombin. This is the first report of a fibrinolytic enzyme that demonstrates additional synergistic activities. This finding accentuates the importance of further development of the enzyme into a powerful agent to treat the thrombus-related disease effectively.
Peptides Hydrolysate Derived from Collagen of Snakehead Murrel (Channa striata) Skin Demonstrate Anti-cholesterol and Anti-oxidant activities Wenny Silvia L. Br. Sinaga; Wangsa T. Ismaya; Debbie S. Retroningrum; Raymond R. Tjandrawinata; Maggy T. Suhartono
HAYATI Journal of Biosciences Vol. 27 No. 2 (2020): April 2020
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (291.388 KB) | DOI: 10.4308/hjb.27.2.136

Abstract

Anti-cholesterol and anti-oxidant play a crucial role to combat cardiovascular disease (CVD), due to formation of arterial plagues from oxidation of cholesterol. In the past decades, bioactive peptides demonstrating anti-cholesterol and anti-oxidant activities have emerged as the alternative drugs. In this study, acid soluble collagen was extracted from the skin of snakehead murrel and employed to induce secretion of collagenase by Bacillus licheniformis F11.4. The collagenases secreted were in turn used to produce peptides hydrolysate and were grouped in two distinct collagenase fractions, designated as fraction D and F. Peptides hydrolysate produced by the fraction D was found to demonstrate HMG-CoA inhibitor activity comparable to pravastatin and limited anti-oxidant activity. Meanwhile, peptides hydrolysate generated using the fraction F demonstrated anti-oxidant activity comparable to BHT (2mM), vitamin C (2mM), and vitamin E (2mM), but limited HMG-CoA activity. Combination of the fraction D and F resulted in substantial HMG-CoA inhibition and anti-oxidant activities.
Overproduction, Purification and Refolding of codon-optimized Hepatitis B Virus X Protein Subgenotype B3 in Escherichia coli BL21(DE3) Anita Artarini; Armini Syamsidi; Anindyajati Anindyajati; Raymond R. Tjandrawinata; Debbie S. Retnoningrum
HAYATI Journal of Biosciences Vol. 29 No. 2 (2022): March 2022
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.29.2.164-170

Abstract

Hepatitis B virus (HBV) infects human and causes chronic liver infection, leading to liver cirrhosis and hepatocellular carcinoma. HBV X (Hbx) protein is known to interact with tumor suppressor protein p53 and block its translocation into the nucleus. This study outlines the overproduction of Hbx protein from HBV subgenotype B3 in Escherichia coli BL21(DE3), including its purification and refolding. The gene encoding Hbx was first codon-optimized and inserted into pET16b. The recombinant plasmid was then transformed into E. coli BL21(DE3) as an expression host. Optimization of Hbx expression was performed with variation of IPTG concentration and overproduction temperature. The results showed that Hbx protein was optimally induced by 0.075 mM IPTG and overproduction of Hbx at 17, 25, and 37°C exhibited no difference in protein level and location. The optimal refolding of Hbx was obtained using 0.1 M arginine prior to elution from Nickel column using 100 mM imidazole and 0.25 M arginine. Hbx migrates differently in SDS-PAGE reducing and non-reducing, while the melting curve pattern in TSA analysis changed after the refolding step. Essentially, this purified Hbx protein could potentially be used for interaction study with p53 and the inhibitor candidate of the protein.
Co-Authors Achmad K. Harzif Agung Endro Nugroho Agung Endro Nugroho Andon Hestiantoro Andri Prasetiyo Anindini Winda Amalia Anindyajati Anindyajati Anita Artarini Armini Syamsidi ARTARINI, ANITA B. Atawolo, Andreas Babu, Murali Mohan Budi Wiweko Caroline G. Puspita CATUR RIANI Danang Agung Yunaidi Dayana, Hepy Debbie S. Retnoningrum Debbie S. Retroningrum DEBBIE SOEFIE RETNONINGRUM Dewi Riskha Nurmalasari Diana Nur Afifah Esti Mumpuni Esti Mumpuni Esti Mumpuni, Esti Gayatri, Anggi Gita Pratama Hapsari, Riani Hartati Tuna, Hartati Heliany, Ina Henry Soelistyo Budi Henry Soelistyo Budi, Henry Soelistyo Herbert Situmorang Herbert Situmorang Huda Shalahudin Darusman Indriawati, Iin Irsan Hasan Ismaya, Wangsa T. Kaka Renaldi Kanadi Sumapradja Krisnayanti, Ni Putu Eka Kristiana, Hery Kristiana, Hery Laurentia Stephani Liana W. Susanto Lilik Sulastri Luh Putu Nurshanti, Ni Maggy T. Suhartono Maggy T. Suhartono Maggy Thenawidjaja Suhartono Marcellus Simadibrata Martha Wijaya, Harry Melva Louisa Murdani Abdullah Nafrialdi Nafrialdi Nailufar, Florensia Nailufar, Florensia Novia Tri Astuti Novia Tri Astuti Novitasari, Putri Rachma Permanasari, Silmi Citra Rachman, Andika Raden Muharam Natadisastra Retroningrum, Debbie S. Santi Tan Saut Horas Hatoguan Nababan Setiabudy, Rahajuningsih D Shirly Kumala SILMI MARIYA Simatupang, Stefeny Theresia Sinaga, Wenny S.L. Soelistyo Budi, Henry Susanto, Liana W Suwijiyo Pramono Suwijiyo Pramono Tan, Santi Viedya Novalinda Said Wangsa T. Ismaya Wangsa Tirta Ismaya Widjaja, Nadia Winoto, Imelda L Winoto, Imelda L Yanti Lim Zaelani, Bella Fatima Dora