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Journal : Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology

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 | Full PDF (617.636 KB) | 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.
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 | Full PDF (1833.689 KB) | 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 | Full PDF (1087.699 KB) | 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.