Biochemical and radical-scavenging properties of sea cucumber (<i>Stichopus vastus</i>) collagen hydrolysates

Abedin, Md. Zainul; Karim, A.A.; Latiff, Aishah A.; Gan, Chee‐Yuen; Ghazali, Farid; Barzideh, Zoha; Ferdosh, Sahena; Jahurul, M.H.A.; Zzaman, Wahidu; Karim, Md. Rezaul; Sarker, Zaidul Islam

doi:10.1080/14786419.2014.900617

Cited by 32 publications

(20 citation statements)

References 23 publications

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“…Collagen does not express antigenicity in physiological conditions, it is completely resorbable in vivo and its physicochemical properties can be suitably controlled. Because of its unique biological and functional properties, collagen has been widely applied in food, cosmetic, base for smart hydrogels and medicine [8][9][10][11][12][13] . At the present there is wide interest in collagen as biomaterials.…”

Section: Introductionmentioning

confidence: 99%

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Rizk¹,

Mostafa²

2016

Orient. J. Chem

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Collagen is widely used for biomedical and pharmaceutical applications due to its excellent biocompatibility, biodegradability and weak antigenicity. However, applicability is limited due to its high cost and probability of disease transmission from the current sources, which are bovine and porcine. In the present study, collagen was extracted from 6 months buffalo skins as alternative save sources. Collagen was characterized by different physico-chemical techniques like ATR-FTIR, Raman, SEM, DSC and amino acids analysis. Proline and hydroxyproline contents of buffalo skin collagen were higher than those of calf skin collagen. Thermal stability of buffalo skin collagen is high with respect to that of calf skin collagen. The obtained buffalo skin collagen shows higher stiffness upon cross-linking with glutaraldehyde. Thus buffalo skin collagen can be used for fabrication of high strength bioactive sponge and sheets for medical applications, like scaffold for tissue engineering, drug delivery and wound dressing system.

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Section: Introductionmentioning

confidence: 99%

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Rizk¹,

Mostafa²

2016

Orient. J. Chem

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“…The biological and functional properties of marine-derived peptides depend on their molecular size, structure and sequence (Najafian and Babji 2012). These properties can be improved by the use of specific enzymes and selection of a defined set of hydrolysis conditions, such as time, pH and temperature, to achieve the desired protein hydrolysates (Abedin et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Sayari

Sila

Haddar

et al. 2015

Environ Sci Pollut Res

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Concerns over the environmental and waste disposal problems created by the large amounts of by-products generated from fish processing industries are increasing worldwide. The bioconversion of those marine waste by-products through the enzymatic hydrolysis of their protein content offers the possibility for the development of bioactive peptides for use in various biotechnological applications. The present study aimed to investigate and evaluate the biological and functional properties of smooth hound (Mustelus mustelus) protein hydrolysates (SHPHs) obtained by treatment with intestinal and gastric enzyme preparations from M. mustelus viscera and porcine pancreatin. The results revealed that the SHPHs exhibited different degrees of hydrolysis and antioxidant activity. The hydrolysate produced by the intestinal crude extract presented the highest rate of antioxidative activity, showing an IC50 value of 1.47 ± 0.07 mg/mL in 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging assays. The alkaline protease extract from the intestine of M. mustelus produced hydrolysate with the highest angiotensin I-converting enzyme (ACE) inhibitory activity (82 ± 1.52% at 2 mg/mL). All the protein hydrolysates showed excellent solubility and interfacial properties that were governed by pH. The major amino acids detected in SHPHs were glutamic acid/glutamine, aspartic acid/asparagine, histidine and arginine, followed by methionine, phenylalanine, serine, valine and leucine. Overall, the results indicated that smooth hound by-products can be used to generate high value-added products, thus offering a valuable source of bioactive peptides for application in wide range of biotechnological and functional food applications.

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“…Trypsin is a serine protease that hydrolyzes peptide chains at the carboxyl side of arginine and lysine residues [28]. In the literature, antioxidative and angiotensin I-converting enzyme (ACE) inhibitory peptides have been identified in tryptic hydrolysates from Nile tilapia skin [29], sea cucumber [30] and whey [31].…”

Section: Research Significancementioning

confidence: 99%

Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activity of Tryptic Spirulina Platensis Protein Hydrolysates: Effect of Hydrolysis and in Vitro Gastrointestinal Digestion

Yücetepe¹,

Kasapoğlu²,

Özçelik³

2018

NWSA

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In this study, protein hydrolysates derived from Spirulina platensis protein (SPPHs) using trypsin were investigated in terms of angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant activity and total phenolic content (TPC) and subjected to an in vitro digestion model using human gastric and duodenal fluids. Moreover, the effects of hydrolysis time and enzyme/substrate (E/S) ratio on the degree of hydrolysis (DH) of the hydrolysates were determined. The maximum DH (%) was found as 25.03±0.89% with the combination of E/S ratio of 3:100, hydrolysis time of 8 hours (p<0.05). The highest ACE inhibitory activity value was observed as 21.79±1.52% for initial SPPHs, prepared within the hydrolysis conditions of E/S ratio of 3:100 and hydrolysis time of 8 h. In general, the increase in E/S ratio and hydrolysis time resulted in an increase in the DH and in an improved ACE inhibitory activity of both initial and the GI digested samples (p<0.05). After digestion by pepsin, TPC of the digests was in the range of 28.87±0.32 and 40.28±1.05mg caffeic acid equivalent/g dry weight. However, further digestion by pancreatin led TPC of the final GI digest between 19.85±1.24 and 29.00±1.00mg caffeic acid equivalent/g dry weight. Moreover, the antioxidant activity of further digested SPPHs by gastric and intestinal proteases remained generally stable after in vitro treatment.

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Biochemical and radical-scavenging properties of sea cucumber (Stichopus vastus) collagen hydrolysates

Cited by 32 publications

References 23 publications

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Valorisation of smooth hound (Mustelus mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides

Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activity of Tryptic Spirulina Platensis Protein Hydrolysates: Effect of Hydrolysis and in Vitro Gastrointestinal Digestion

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