ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

Mahmoodani, Fatemeh; Ghassem, Masomeh; Babji, Abdul Salam; Yusop, Salma Mohamad; Khosrokhavar, Roya

doi:10.1007/s13197-012-0742-8

Cited by 36 publications

(21 citation statements)

References 62 publications

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“…2011a) and fish gelatine hydrolysates (Mahmoodani et al . ). Although the ACE inhibitory activity of both peptides decreased by further digestion of peptide hydrolysates by mucosal peptidase (lower intestinal peptidase), the differences were not significant (Table ).…”

Section: Resultsmentioning

confidence: 97%

Angiotensin I-Converting Enzyme Inhibitory Peptides from Snakehead Fish Sarcoplasmic Protein Hydrolysate

Ghassem

Babji

Said

et al. 2013

Journal of Food Biochemistry

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In this study, the angiotensin I-converting enzyme (ACE) inhibitory peptides were isolated from snakehead fish sarcoplasmic protein hydrolysates. Enzymatic hydrolysis of sarcoplasmic protein was performed using various commercial enzymes. The alcalase hydrolysate with the highest ACE inhibition activity was purified with gel chromatography and reversed phased high-performance liquid chromatography. The purified fractions were then subjected to electrospray ionization quadrupole-micro-time-of-flight mass spectrometry for amino acid characterization. Two novel ACE inhibitory peptides LYPPP and YSMYPP with IC50 values of 1.3 and 2.8 mM were identified, respectively. The pattern of ACE inhibition, resistance to hydrolysis by gastrointestinal proteases and cytotoxic potencies of isolated peptides were described. The results showed no cytotoxicity of peptides on human embryonic fibroblast cell line (MRC-5) and human hepatocarcinoma cell line (HepG2). PRACTICAL APPLICATIONSFreshwater fish muscle proteins and their hydrolysates offer huge potential as novel sources of natural bioactive peptides with angiotensin I-converting enzyme (ACE) inhibitory activity. The present study revealed the identification of two strong ACE inhibitory peptides obtained from alcalase hydrolysis of snakehead fish sarcoplasmic protein. However, further studies are required to determine the in vivo antihypertensive activity of the purified potent ACE inhibitory peptides. bs_bs_banner Journal of Food Biochemistry ISSN 1745-4514 ACE INHIBITORS OF SNAKEHEAD SARCOPLASMIC PROTEIN HYDROLYSATE M. GHASSEM ET AL.

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Section: Resultsmentioning

confidence: 97%

Angiotensin I-Converting Enzyme Inhibitory Peptides from Snakehead Fish Sarcoplasmic Protein Hydrolysate

Ghassem

Babji

Said

et al. 2013

Journal of Food Biochemistry

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“…It is because the fish based gelatin could be potential to replace the mammalian gelatin, which is the most source of gelatin however unacceptable due to religion, sociocultural and health aspect consideration (Nurul and Sarbon 2015). Many previous studies have been reported that the fish gelatins have their bioactivities, for example, the gelatin from salmon, hake, halibut, nila tilapia, pangasius catfish and etc (Li-Chan et al 2012;Mahmoodani et al 2014a;Wang et al 2015). Fortunately, most of fish based gelatin comes from by-product or waste of fish processing (Karayannakidis and Zotos 2016).…”

Section: Introductionmentioning

confidence: 99%

The hydroxyproline content of fish bone gelatin from Indonesian Pangasius catfish by enzymatic hydrolysis for producing the bioactive peptide

et al. 2018

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Abstract. Atma Y, Lioe HN, Prangdimurti E, Seftiono H, Tahufik M, Fitriani D, Mustopa AZ. 2018. The hydroxyproline content on fish bone gelatin from Indonesian Pangasius catfish by enzymatic hydrolysis for producing of bioactive peptide. Biofarmasi J Nat Prod Biochem 16: 64-68. Gelatins has been widely used in food, medicines, cosmetics, photography industries. In the food industry, gelatin used as food additives and functional foods. The applications of gelatin as a functional food due to their bioactivity in a form of peptides. Bioactive peptides from gelatin are mostly obtained through enzymatic hydrolysis processes. This study was conducted to measure the hydroxyproline content of gelatin bone of Indonesian Pangasius catfish (Pangasius sutchi) before and after enzymatic hydrolysis. The hydroxyproline is one of the dominant amino acids in gelatin. Gelatin hydrolysis was carried out using a flavourzyme at concentration of 6% and the incubation series of 0, 4, 6 and 8 hours. The standard concentration of hydroxyproline was used in range of 0-1 μg. The results showed that the linear curve of the hydroxyproline standard solution was y=0.0554x+0.0406, with the coefficient of determination (R²) = 0.9435. The incubation time of enzymatic hydrolysis (6% enzyme concentration) affected the hydroxyproline content. The hydroxyproline from fish bone gelatin was 18.91±2.87 mg/mL, 63.81±1.28 mg/mL, 46.21±1.28 mg/mL and 37.64 ± 0.64 mg/mL respectively during 0, 4, 6 dan 8 h incubation time. This hydroxyproline content was significantly different at 95% confidence level from each treatment time.

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“…Then, adjusted to pH 7.0 with addition of 1 M NaOH and centrifugated (Hettich, Tuttlingen, Germany) at 10.000 g, 4 o C for 15 minutes. The supernatant or gelatin hydrolysate was collected and stored at -18 o C. The degree of hydrolysis (DH) measured by quantify of remain protein in hydrolysate divided total protein in gelatin (whitout hydrolysis) as adopted from Mahmoodani et al [26] which is using 20% Trichloroacetic acid (TCA) (w/v) to allow precipitation, Bradford solution (commasie brilliant blue G250:ethanol :phosphoric acid; 2:1:2; w/v/v) to protein quantification and Bovine serum albumin (0.1-1 mg/mL) to determine standard qurve.…”

Section: Gelatin Hydrolysismentioning

confidence: 99%

Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

Atma¹,

Lioe²,

Prangdimurti³

et al. 2019

Int. J. Adv. Sci. Eng. Inf. Technol.

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Bioactive peptides have been investigated largely for many biofunctional properties. The aim of this research was to determine the inhibitory activity of ultrafiltration (UF) and gel filtration (GF) fractions of gelatin derived from bone of Pangasius catfish against dipeptidyl peptidase IV (DPP-IV). Previous studies have shown that gelatin from skins of salmon, hake, halibut, milkfish, tilapia and bone of pangasius catfish have the activity in DPP-IV inhibition. While, as inhibitor, most of previous and recent studies shown that separation and fractination of gelatin hydrolysate increase their activity. This research was conducted in three stages including gelatin hydrolysates fractination by ultrafiltration (UF), UF fraction loaded into gel filtration (GF) and DPP-IV inhibition measurement. The fish bone gelatin was hydrolyzed using flavourzyme at three enzyme/substrate ratios (E/S of 3%, 6% and 9%) with incubation times 4, 6, and 8 h. Then, the hydrolysates fractioned by ultrafiltration with 3 kDa cutoff membrane continued with Superfine G-25 sephadex column (65 cm x 3 cm, flow rate 1 mL/min). The result shown that both group of fractions i.e UF and GF have inhibitory activity regarding their capacity to inhibit DPP-IV. The UF fraction >3 kDa derived from 9% (E/S) ratio for hdyrolysis were superb as DPP-IV inhibitor than other fractions, the highest one also has bioactivity higher than other previous fish gelatin fractions.

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ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

Cited by 36 publications

References 62 publications

Angiotensin I-Converting Enzyme Inhibitory Peptides from Snakehead Fish Sarcoplasmic Protein Hydrolysate

Angiotensin I-Converting Enzyme Inhibitory Peptides from Snakehead Fish Sarcoplasmic Protein Hydrolysate

The hydroxyproline content of fish bone gelatin from Indonesian Pangasius catfish by enzymatic hydrolysis for producing the bioactive peptide

Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

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