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AKTIVITAS ANTIBAKTERI DAN ANTIOKSIDAN HIDROLISAT HASIL HIDROLISIS PROTEIN SUSU KAMBING DENGAN EKSTRAK KASAR BROMELIN Kusumaningtyas, Eni; Widiastuti, Raphaella; Kusumaningrum, Harsi Dewantari; Suhartono, Maggy Thenawidjaja
Jurnal Teknologi dan Industri Pangan Vol. 26 No. 2 (2015): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (460.557 KB) | DOI: 10.6066/jtip.2015.26.2.179

Abstract

Goat milk is highly nutritious foodstuffs that beneficial for improving health. The milk contains bioactive peptides which produced by hydrolysis process. The aim of this study was to evaluate antibacterial and antioxidant activities of hydrolisate produced from hydrolysis of goat milk protein by crude bromelain extract. Hydrolysis of goat milk protein was conducted using crude bromelain (0.1 U/mL) at pH 6, 50°C for 60 min. Hydrolysate was fractionated by using membrane molecular weight cut off 10 kDa. hydrolysate before and after fractionation were assayed for antibacterial and antioxidant activities. Toxicity of the Hydrolysate was determined by hemolysis assay. The result showed that the hydrolysate before and after fractionation inhibited growth of E. coli, S. Typhimurium and L. monocytogenes. Hydrolysate after fractionation has higher antibacterial activity indicated that fractionation was able to improve antibacterial activities of the hydrolysate fraction. The hydrolysate showed scavenging activity to ABTS and DPPH radicals. Fraction <10 kDa has the highest antioxidant activity against both ABTS and DPPH radicals. Hemolysis assay showed that hydrolysate before and after fractionation did not cause lysis of red blood cells, indicating safe for application. Both fraction <10 kDa and >10 kDa not only showed absence of hemolysis but also they were able to reduce autolysis of red blood cells. The result showed that hydrolysate from goat milk hydrolyzed by bromelain were able to be antibacterial and antioxidant.
FOOD ORIGIN FIBRINOLYTIC ENZYME WITH MULTIPLE ACTIONS Stephani, Laurentia; Tjandrawinata, Raymond Rubianto; Afifah, Diana Nur; Lim, Yanti; Ismaya, Wangsa Tirta; Suhartono, Maggy Thenawidjaja
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.
IMUNOMODULATOR ACTIVITY OF ALGINATE OLIGOSACCHARIDES FROM ALGINATE SARGASSUM CRASSIFOLIUM Subaryono, Subaryono; Perangiangin, Rosmawati; Suhartono, Maggy Thenawidjaja; Zakaria, Fransiska Rungkat
Jurnal Pengolahan Hasil Perikanan Indonesia Vol. 20 No. 1 (2017): Jurnal Pengolahan Hasil Perikanan Indonesia
Publisher : Department of Aquatic Product Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (690.154 KB) | DOI: 10.17844/jphpi.v20i1.16434

Abstract

Alginate oligosaccharides (AOS) are oligosaccharides produced from depolimerization of the alginate polymer, and is reported to have various biological activities. The study aims is to determine the effect of AOSproduction conditions and their effects on products and its activities as an immunomodulatory compound. Production of alginate oligosaccharides (AOS) enzymatically carried out with the help of alginate lyase enzyme produced from the bacterium Bacillus megaterium S245. Variation of incubation time is 2, 4, 6 and 8 hours at concentrations of alginate lyase enzyme addition of 25, 50, 75 and 100U. Treatment of enzyme concentration and the duration of incubation in the production of AOS produces a degree of polymerization (DP) 2-7. In vitro activity test showed AOS is have ability to induce cell proliferation of human lymphocytes.This type of cell lymphocytes proliferation induced by AOS is a CD 8 cells or cytotoxic T cell and non cell CD4 / CD8. AOS production conditions with the addition of alginate lyase enzyme 50 U and incubation period 2 hours has produce AOS with the highest index of lymphocyte proliferation  117.6+3.6% or an increase of 43.24% compared to the native alginat polymer.
Isolasi dan Identifikasi Bakteri Asam Laktat Penghasil Inhibitor Enzim HMG-KoA Reduktase dari Bekasam Sebagai Agen Pereduksi Kolesterol Rinto, Rinto; Dewanti, Ratih; Yasni, Sedarnawati; Suhartono, Maggy Thenawidjaja
Agritech Vol 35, No 3 (2015)
Publisher : Faculty of Agricultural Technology, Universitas Gadjah Mada, Yogyakarta, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (637.273 KB) | DOI: 10.22146/agritech.9342

Abstract

The purpose of this research was to obtain statins producer bacteria as a HMG-CoA reductase (HMGR) enzyme inhibitor to reduced cholesterol biosynthesis. Stages of this research were the isolation of compactin and lovastatin resistant bacteria, statin production, analysis of culture extracts to inhibition of HMG-CoA reductase and identification of bacteria. The results showed that the 20 isolates of compactin and lovastatin resistant bacteria, there are 5 bacterial isolates produced statins. They were L3.3.4; C3.4.2; C3.3.5; C3.4.4 and L3.3.3; with the statins content were 9.491; 1.536; 0.065; 0.060; and 0.040 ppm. Selection of the 5 bacterial isolates resulted 2 bacteria which had inhibition ability to HMGR enzyme activity. They were Lactobacillus acidophilus and Lactobacillus delbruckii sp. delbruckii with inhibitory ability were 66.67% and 58.33%, respectively.ABSTRAKPenelitian ini bertujuan memperoleh bakteri penghasil statin sebagai inhibitor enzim HMG-KoA reduktase (HMGR), penghambat sintesis kolesterol. Tahapan penelitian yang dilakukan adalah isolasi bakteri yang resisten terhadap compactin dan lovastatin, produksi statin, uji penghambatan ekstrak dari kultur bakteri terhadap HMG-KoA reduktase dan identifikasi bakteri. Hasil penelitian menunjukan bahwa dari 20 isolat bakteri yang resisten terhadap compactin maupun lovastatin, terdapat 5 isolat bakteri yang potensial menghasilkan statin, yaitu isolat L3.3.4; C3.4.2; C3.3.5; C3.4.4 dan L3.3.3; dengan kandungan statin berturut-turut adalah 9.491; 1,536; 0,065, 0,060, dan 0,040 ppm. Seleksi terhadap 5 isolat menghasilkan 2 bakteri yang mempunyai kemampuan penghambatan terhadap aktivitas enzim ¸Â•ÝWtu Lactobacillus acidophilus dan Lactobacillus delbruckii sp. delbruckii dengan kemampuan penghambatan  berturut-turut adalah 66,67% dan 58,33%.
Angiotensin Converting Enzyme (ACE) Inhibitory Activity of Crude and Fractionated Snakehead Fish (Channa striata) Fillet Extract Budiari, Setyani; Chasanah, Ekowati; Suhartono, Maggy Thenawidjaja; Palupi, Nurheni Sri
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 13, No 2 (2018): August 2018
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.v13i2.345

Abstract

The existence of endogenous bioactive protein or peptide with angiotensin-converting enzyme (ACE) inhibitory activity in snakehead fish fillet is promising to be investigated. The purposes of this research were to extract ACE inhibitory endogenous protein or peptide from snakehead fish fillet and to fractionate the active compounds using ultrafiltration. The extraction employed two solvents, i.e. aquadest and 50% ethanol. Fractionation was conducted using ultrafiltration membranes of 10,000; 5,000 and 3,000 Molecular Weight Cut Off  (MWCO) to separate the protein or peptide into the sizes of >10 kDa, 5-10 kDa, 3 -5 kDa and <3 kDa. The parameters observed were protein and peptide content, ACE inhibitory activity (in vitro) and also protein and peptide profiles. The result revealed that the snakehead fish fillet contained ACE inhibitory endogenous bioactive protein or peptide. The 50% ethanol was more effective in extracting peptide of <10 kDa than the aquadest. Yet, the aquadest was better in extracting higher molecular weight protein of >10 kDa than the 50% ethanol. The fraction of <3 kDa by aquadest had the highest ACE inhibitor activity per g protein (7.85% inhibition of ACE per g protein). Thus, the fraction of <3 kDa aquadest is the most promising option for further research and development of natural anti-hypertension compound. From the result, snakehead fish fillet was potential to be utilized as a functional food as well as functional ingredient to fight hypertension.
Sequences Analysis of a Gene Encoding Extracellular Xylanase in Streptomyces costaricanus 45I-3 Sipriyadi, S.; Wahyudi, Aris Tri; Suhartono, Maggy Thenawidjaja; Meryandini, Anja
Indonesian Journal of Biotechnology Vol 20, No 1 (2015)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (314.446 KB) | DOI: 10.22146/ijbiotech.15274

Abstract

Streptomyces costaricanus 45I-3 is a bacterial strain belongs to actinomycetes group isolated from peat soil. Thebacterium is known to produce extracellular xylanase. The aims of this study were to analyze DNA sequence andsub-clone gene involved in the synthesis of extracellular xylanase. Complete DNA sequence predicted to encodexylanase genes was isolated from bacterial genome using Inverse Polymerase Chain Reaction (I-PCR). Total DNAsequence of 1664 bp in size obtained from I-PCR consisted of two open reading frames (ORF) in opposite direction.ORF1 was 1029 bp and ORF2 (partial sequence) was 309 bp. Analysis sequence using BlastX indicated that ORF1was homologous with xylanase bacterium enrichment culture clone Xyl8B8 (GenBank accession No. AFH35005.1),i.e. 95% in identity and 99% in similarity. In addition, ORF2 was homologous with glyoxalase bacterium enrichmentculture clone Xyl8B8 (GenBank accession No. AFH35007.1), i.e. 95% in identity and 98% in similarity. Analysis ofamino acid sequence revealed that ORF1 consisted of 2 domains, i.e. glyco-hydrolase 11 (GH11) and CarbohydrateBinding Type 2 (CBM2). Active site was found at 130th amino acid on GH11 domain. Visualization of 3-dimensionstructure showed that 1029 bp fragment is of 19 areas.
Alginate Lyase from Indonesian Bacillus megaterium S245 Shows Activities Toward Polymannuronate and Polyguluronate Subaryono, Subaryono; Ardilasari, Yuwanita; Peranginangin, Rosmawaty; Zakaria, Fransisca Rungkat; Suhartono, Maggy Thenawidjaja
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 11, No 2 (2016): August 2016
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.v11i2.250

Abstract

Screening of alginate lyase producing bacteria associated with seaweed Sargassum crassifolium was carried out, and isolate S245, identified as Bacillus megaterium S245 was found to produce high alginate lyase activity. This research was conducted to evaluate activity of the alginate lyase enzyme at various pHs, temperatures and substrates. Polymannuronate and polyguluronate were used to evaluate substrate specificities. Alginate lyase activity was assayed by analysis of reducing sugar released using the 3,5 dinitrosalicylic acid (DNS) method. The research showed that the activity of alginate lyase was optimum at pH of 7.0 and  temperature of 45 0C. This enzyme was active for both polymannuronate and polyguluronate susbtrates. The Vmax and Km of this enzyme for polymannuronate and polyguluronate were 200 unit/ml/min and 79.8 mg/ml for polymannuronate substrate and 27.78 unit/ml/min and 13.17 mg/ml for polyguluronate substrate. This enzyme showed unique characteristic in working toward the two substrates.
Alginate Lyases: Sources, Mechanism of Activity and Potencial Application Subaryono, Subaryono; Peranginangin, Rosmawaty; Suhartono, Maggy Thenawidjaja; Zakaria, Fransiska Rungkat
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 8, No 3 (2013): December 2013
Publisher : Research and Development Center for Marine and Fisheries Product Processing and Biotechnol

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.v8i3.39

Abstract

Alginate lyases are group of enzymes which catalyze depolymerization of alginate into oligosaccharides. Alginate lyase have been widely used in many applications such as in production of bioactive oligosaccharides, control of polysaccharide rheological properties, and polysaccharide structure analysis. The products of alginate lyase, polysaccharide structure analysis, alginate oligosaccharides (AOS) have many biological activities including act as prebiotics, immune modulator, anticoagulation, antioxidant, anticancer, growth promoting activities, promote production of antibiotics and ethanol. In relation to the importance of alginate lyases, their potential aplications and prospect in development of new bioactive products, we present review of the enzymes, sources, mechanism of activity and potential applications. This paper also discussed some new biological engineering in alginate lyase production.
PRODUCTION AND CHARACTERIZATION OF CHITINASE ENZYMES FROM SULILI HOT SPRING IN SOUTH SULAWESI, Bacillus sp. HSA,3-1a Natsir, Hasnah; Patong, Abd. Rauf; Suhartono, Maggy Thenawidjaja; Ahmad, Ahyar
Indonesian Journal of Chemistry Vol 10, No 2 (2010)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (591.606 KB) | DOI: 10.22146/ijc.21470

Abstract

Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 °C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 °C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 °C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were  decreased by 1 mM Co2+, Fe2+ and Zn2 ions. The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa.   Keywords: colloidal chitin, thermophilic bacteria, chitinase
Exploration of Potential Actinomycetes from CIFOR Forest Origin as Antimicrobial, Antifungus, and Producing Extracellular Xylanase Sipriyadi, Sipriyadi; Lestari, Yulin; Wahyudi, Aris Tri; Meryandini, Anja; Suhartono, Maggy Thenawidjaja
Biosaintifika: Journal of Biology & Biology Education Vol 8, No 1 (2016): March 2016
Publisher : Department of Biology, Faculty of Mathematics and Sciences, Semarang State University . Ro

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15294/biosaintifika.v8i1.5052

Abstract

This study aimed to isolate and explore the actinomycetes of CIFOR forest origin as an antimicrobial and antifungal agent, to produce an extracellular xylanase, and to identify isolates based on 16S rRNA gene sequences. Actinomycetes were isolated using Humic-acid Vitamin-B agar (HV) media. Actinomycetes colonies that grow on the medium HV was subsequently purified by growing them on yeast malt agar (YMA) media), then an antagonistic test of selected bacteria against Bacillus sp., Escherichia coli, Fusarium oxysporum, and Sclerotium sp was performed. Xylanase activity test was detected by observing a clear zone, followed by identification. Total of 35 isolates of actinomycetes isolated based on their colony morphology characteristics and diverse types of spore chains showed Streptomyces spp. of isolates CFR-06, CFR-15, CFR-17, CFR-18, and CFR-19 were able to inhibit the growth of Bacillus sp.. The highest inhibition zone has a diameter of 10.1 mm (isolate CFR-17). Isolates CFR-01 and CFR-15 were able to inhibit the growth of E. coli with the highest inhibition zone diameter of 5.1 mm (isolate CFR-15). Isolates CFR-29 and CFR-12 were able to inhibit the growth of F. oxysporum while isolate CFR-35 were able to inhibit the growth of Sclerotium sp.. Xylanase activity test showed that isolates CFR-12, CFR-20, CFR-22, CFR-24, CFR-25, CFR-30, CFR-33, CFR-34 have an ability to produce extracellular xylanase enzyme. Actinomycetes isolate (Xyl_22) as a potential xylanase enzyme producer was closely related with Streptomyces drozdowicii by the maximum similarity of 99%.How to CiteSipriyadi, S., Lestari, Y., Wahyudi, A., Meryandini, A., & Suhartono, M. T. (2016). Exploration Potential CIFOR Forest actinomycetes origin as Antimicrobial, Anti Fungus and Producing Enzymes Extracellular Xylanase. Biosaintifika: Journal of Biology & Biology Education, 8(1), 94-102.