Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects

Mendis, Eresha; Rajapakse, Niranjan; Byun, Hee‐Guk; Kim, Se‐Kwon

doi:10.1016/j.lfs.2005.03.016

Cited by 452 publications

(278 citation statements)

References 23 publications

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“…It is thought that collagen can inactivate reactive oxygen species, reduce hydroperoxides, enzymatically eliminate specific oxidants, chelate pro-oxidative transition metals and scavenge free radicals, which may contribute to their antioxidant activities . Moreover, certain specific amino acid residues and their sequences are thought to be responsible for antioxidant activities (Mendis et al 2005). In the present study, higher content of hydrophobic amino acids (valine, leucine and isoleucine) and glycoprotein content in CIIp than that of CII also supports the superior antioxidant activity of CIIp.…”

Section: Antioxidant Activitysupporting

confidence: 71%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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A low molecular weight type-II collagenous polypeptide (CIIp) from whale shark (WS) cartilage was prepared by thermolysin digestion; and examined for their physico-functional and antioxidant properties. The purified collagen was composed of an identical (α 1 ) 3 chains and was characterized as type-II. After hydrolysis with thermolysin, the α-chain of the WS collagen was degraded into smaller peptides with molecular weight ranging from 70 to 20KDa. CIIp was successfully separated from the hydrolysates with molecular weight of approximately 37 kDa. Amino acid analysis of CII, and CIIp indicated imino acid contents of 155 and 121 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CII and CIIp were observed, which suggested that the hydrolysis process by thermolysin affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of CII (34°C) was higher than that of CIIp. Low content of glycoprotein was observed in CII than CIIp due to removal of some polypeptides by thermolysin digestion. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIp was greater than that of CII. The results proposed that the purified CIIp from WS cartilage with excellent antioxidant activities could be the suitable biomaterial for therapeutic applications.

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Section: Antioxidant Activitysupporting

confidence: 71%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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“…Control plates devoid of nanoparticles did not exhibit any inhibition zones. Bacterial inhibition may be due to the release of free radical from the surface of the AgNp that attacks the membrane lipids and then lead to a breakdown of membrane function [23]. Previous studies, using a 6 mg/mL nanoparticle concentration, have found the ZOI to be between 12 and 13.6 mm for both ciprofloxacin-resistant and non-resistant strains of P. aeruginosa [24], but our results, using around 7 mg of nanoparticles, gave a much larger ZOI of about 15 mm.…”

Section: Disc Diffusion Methodsmentioning

confidence: 99%

Ipomea carnea-based silver nanoparticle synthesis for antibacterial activity against selected human pathogens

Daniel

Bayyurt

Muthukumar

et al. 2012

Journal of Experimental Nanoscience

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“…A number of commercial proteases have been used for the production of these hydrolysates and peptides (Lin and Li 2006;Mendis et al 2005;Yang et al 2008). Protease specificity affects size, amount, free amino acid composition and, peptides and their amino acid sequences, which in turn influences the biological activity of the hydrolysates (Chen et al 1995;Jeon et al 1999;Wu et al 2003).…”

Section: Degree Of Hydrolysis (%)mentioning

confidence: 99%

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

et al. 2012

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Skin and bone gelatins of pangasius catfish (Pangasius sutchi) were hydrolyzed with alcalase to isolate Angiotensin Converting Enzyme (ACE) inhibitory peptides. Samples with the highest degree of hydrolysis (DH) were separated into different fractions with molecular weight cutoff (MWCO) sizes of 10, 3 and 1 kDa, respectively and assayed for ACE inhibitory activity. Skin and bone gelatins had highest DH of 64.87 and 68.48 % after 2 and 1 h incubation, respectively. Results from this study indicated that by decreasing the molecular weight of fractions, ACE inhibitory activity was increased. Therefore, F 3 permeates (MWCO< 1 kDa) of skin (IC 50 03.2 μg/ml) and bone (IC 50 01.3 μg/ml) gelatins possessed higher ACE inhibitory activity compared to their untreated gelatins and corresponding hydrolyzed fractions. In this study, the major amino acids were Glycine followed by Proline with an increased amount of hydrophobic amino acid content in F 3 permeates of skin (4.01 %) and bone (5.79 %) gelatin. Digestion stability against gastrointestinal proteases did not show any remarkable change on ACE inhibition potency of these permeates. It was concluded that alcalase hydrolysis of P. sutchi by-products could be utilized as a part of functional food or ingredients of a formulated drug in order to control high blood pressure.

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Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects

Cited by 452 publications

References 23 publications

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Ipomea carnea-based silver nanoparticle synthesis for antibacterial activity against selected human pathogens

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

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