Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
Mar Drugs
2019 Mar 15;173:. doi: 10.3390/md17030169.
Show Gene links
Show Anatomy links
Preparation and Evaluation of Peptides with Potential Antioxidant Activity by Microwave Assisted Enzymatic Hydrolysis of Collagen from Sea Cucumber Acaudina Molpadioides Obtained from Zhejiang Province in China.
Jin HX, Xu HP, Li Y, Zhang QW, Xie H.
???displayArticle.abstract???
The present study was focused on the preparation and characterization of the antioxidant peptides by microwave-assisted enzymatic hydrolysis of collagen from sea cucumber Acaudina molpadioides (ASC-Am) obtained from Zhejiang Province in China. The results exhibited the effects of microwave irradiation on hydrolysis of ASC-Am with different protease. Neutrase was selected from the four common proteases (papain, pepsin, trypsin, and neutrase) based on the highest content and DPPH scavenging activity of hydrolysate Fa (Molecular weight < 1 kDa). The content and 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity of Fa obtained by hydrolysis of neutrase increased by 100% and 109% respectively at a microwave power of 300 W compared with no microwave irradiation. Five subfractions were obtained after performing the gel filtration chromatography, and the Fa.2 exhibited the highest DPPH scavenging activity. The amino acid analysis showed that the contents of Glutamic acid, Alanine, Tyrosine, and Phenylalanine in fraction Fa.2 increased significantly, but an obvious decrease in the content of Glycine was observed compared to Fa. Four peptides (Fa.2-A, Fa.2-B, Fa.2-C, and Fa.2-D) were purified from Fa.2 by high performance liquid chromatography, and Fa.2-C showed the highest DPPH scavenging activity. The sequence of Fa.2-C was identified as Phenylalanine-Leucine- Alanine-Proline with a half elimination ratio (EC50) of 0.385 mg/mL. The antioxidant activity of Fa.2-C was probably attributed to the small molecular sizes and the presence of hydrophobic amino acid residues in its sequence. This report provided a promising method for the preparation of antioxidant peptides from collagen for food and medicinal purposes.
Figure 1. Effect of microwave power on contents (a) and DPPH scavenging activities (b) of Fa (â ), Fb (â ), and Fc (â ) from hydrolysate of ASC-Am by papain. The experiment was performed in triplicate within three days with the same collagen obtained from the same batch of sea cucumber. All values were the mean ± standard deviation (SD).
Figure 2. Effect of microwave power on contents (a) and DPPH scavenging activities (b) of Fa (â ), Fb (â ), and Fc (â ) from hydrolysate of ASC-Am by pepsin. The experiment was performed in triplicate within three days with the same collagen obtained from the same batch of sea cucumber. All values were the mean ± standard deviation (SD).
Figure 3. Effect of microwave power on contents (a) and DPPH scavenging activities (b) of Fa (â ), Fb (â ), and Fc (â ) from hydrolysate of ASC-Am by trypsin. The experiment was performed in triplicate within three days with the same collagen obtained from the same batch of sea cucumber. All values were the mean ± standard deviation (SD).
Figure 4. Effect of microwave power on contents (a) and DPPH scavenging activities (b) of Fa (â ), Fb (â ), and Fc (â ) from hydrolysates of ASC-Am by neutrase. The experiment was performed in triplicate within three days with the same collagen obtained from the same batch of sea cucumber. All values were the mean ± standard deviation (SD).
Figure 5. Effect of microwave time on contents (a) and DPPH scavenging activities (b) of Fa (â ), Fb (â ), and Fc (â ) from hydrolysates of ASC-Am by neutrase. The experiment was performed in triplicate within three days with the same collagen obtained from the same batch of sea cucumber. All values were the mean ± standard deviation (SD).
Figure 6. Effect of Fa (â, â) and ascorbic acid (â , â ) concentrations on DPPH radical (â, â ) and ABTS radical (â, â ) scavenging activity. Fa was the hydrolysate (Mw < 1 kDa) by neutrase hydrolysis of ASC-Am at 300 W for 30 min. The experiment was performed in triplicate within three days with the same sample of Fa. All values were the mean ± standard deviation (SD). (aâe) Values with different letters indicated significant differences in the same free radical at different concentrations (p < 0.05); (AâB) Values with different letters indicated significant differences in the different free radical at the same concentration (p < 0.05).
Figure 7. (a) Separation scheme of antioxidant peptide from Fa by Sephadex G-25 column; (b) The DPPH scavenging activity of fractions from Fa at concentration of 0.2 mg/mL. Fa was the hydrolysate (Mw < 1 kDa) by neutrase hydrolysis of ASC-Am at 300 W for 30 min. The experiment was performed in triplicate within three days with the same sample of Fa. All values were the mean ± standard deviation (SD). (aâd) Values with different letters indicated significant differences in the different sample at same concentrations (p < 0.05).
Figure 8. RP-HPLC chromatography of Fa.2 on Zorbax. SB C-18 column (a) and the DPPH scavenging activity of four peptides at concentration of 0.2 mg/mL (b). Fa.2 was isolated from the hydrolysate Fa obtained by neutrase hydrolysis of ASC-Am at 300 W for 30 min. The experiment was performed in triplicate within three days with the same sample of Fa.2. (aâd) Values with different letters indicated significant differences in the different sample at same concentrations (p < 0.05).
Abedin,
Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus).
2013, Pubmed,
Echinobase
Abedin,
Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus).
2013,
Pubmed
,
Echinobase Adibzadeh,
Purification and characterization of pepsin-solubilized collagen from skin of sea cucumber Holothuria parva.
2014,
Pubmed
,
Echinobase Ao,
Amino acid composition and antioxidant activities of hydrolysates and peptide fractions from porcine collagen.
2012,
Pubmed Bordbar,
High-value components and bioactives from sea cucumbers for functional foods--a review.
2011,
Pubmed
,
Echinobase Buehler,
Nature designs tough collagen: explaining the nanostructure of collagen fibrils.
2006,
Pubmed Chi,
Influence of Amino Acid Compositions and Peptide Profiles on Antioxidant Capacities of Two Protein Hydrolysates from Skipjack Tuna (Katsuwonus pelamis) Dark Muscle.
2015,
Pubmed Chi,
Purification and characterization of three antioxidant peptides from protein hydrolyzate of croceine croaker (Pseudosciaena crocea) muscle.
2015,
Pubmed Herod,
Collagen fibrils in functionally distinct tendons have differing structural responses to tendon rupture and fatigue loading.
2016,
Pubmed Himaya,
Peptide isolated from Japanese flounder skin gelatin protects against cellular oxidative damage.
2012,
Pubmed Huang,
Antioxidant activity measurement and potential antioxidant peptides exploration from hydrolysates of novel continuous microwave-assisted enzymolysis of the Scomberomorus niphonius protein.
2017,
Pubmed Ilyas,
Microwave-assisted synthesis and evaluation of type 1 collagen-apatite composites for dental tissue regeneration.
2018,
Pubmed Iwai,
Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates.
2005,
Pubmed Jang,
Hydrolysis conditions for antioxidant peptides derived from enzymatic hydrolysates of sandfish (Arctoscopus japonicus).
2017,
Pubmed Jiang,
Purification and characterization of antioxidative peptides from round scad (Decapterus maruadsi) muscle protein hydrolysate.
2014,
Pubmed Lin,
Antioxidative peptides derived from enzyme hydrolysis of bone collagen after microwave assisted acid pre-treatment and nitrogen protection.
2010,
Pubmed Liu,
A comparative study of the properties and self-aggregation behavior of collagens from the scales and skin of grass carp (Ctenopharyngodon idella).
2018,
Pubmed Mar,
Simultaneous extraction of arsenic and selenium species from rice products by microwave-assisted enzymatic extraction and analysis by ion chromatography-inductively coupled plasma-mass spectrometry.
2009,
Pubmed Matsuda,
Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis.
2006,
Pubmed Mendis,
Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate.
2005,
Pubmed Minaguchi,
Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in Achilles tendon.
2005,
Pubmed Ohara,
Effects of Pro-Hyp, a collagen hydrolysate-derived peptide, on hyaluronic acid synthesis using in vitro cultured synovium cells and oral ingestion of collagen hydrolysates in a guinea pig model of osteoarthritis.
2010,
Pubmed Park,
Pepsin-solubilised collagen (PSC) from Red Sea cucumber (Stichopus japonicus) regulates cell cycle and the fibronectin synthesis in HaCaT cell migration.
2012,
Pubmed
,
Echinobase Pownall,
Amino acid composition and antioxidant properties of pea seed ( Pisum sativum L.) enzymatic protein hydrolysate fractions.
2010,
Pubmed Rajapakse,
Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems.
2005,
Pubmed Saiga,
Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment.
2003,
Pubmed Tanaka,
Effects of collagen peptide ingestion on UV-B-induced skin damage.
2009,
Pubmed Venkatesan,
Marine Fish Proteins and Peptides for Cosmeceuticals: A Review.
2017,
Pubmed Wan,
Nonthermal effect of microwave irradiation in nonaqueous enzymatic esterification.
2012,
Pubmed Wang,
Isolation and characterization of collagen and antioxidant collagen peptides from scales of croceine croaker (Pseudosciaena crocea).
2013,
Pubmed Wang,
Preparation and evaluation of antioxidant peptides from ethanol-soluble proteins hydrolysate of Sphyrna lewini muscle.
2012,
Pubmed Wang,
Purification and characterisation of a novel antioxidant peptide derived from blue mussel (Mytilus edulis) protein hydrolysate.
2013,
Pubmed Wattanasiritham,
Isolation and identification of antioxidant peptides from enzymatically hydrolyzed rice bran protein.
2016,
Pubmed Wu,
Assessment of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats.
2004,
Pubmed Wu,
[Preparation and antioxidant activity detection of collagen peptide from Cirrhinus molitorella skin].
2016,
Pubmed Zhang,
Characterisation of acid-soluble and pepsin-solubilised collagen from jellyfish (Cyanea nozakii Kishinouye).
2014,
Pubmed Zhang,
Optimization of a microwave-coupled enzymatic digestion process to prepare peanut peptides.
2012,
Pubmed Zhao,
Preparation, Physicochemical and Antioxidant Properties of Acid- and Pepsin-Soluble Collagens from the Swim Bladders of Miiuy Croaker (Miichthys miiuy).
2018,
Pubmed Zhong,
Isolation and characterization of collagen from the body wall of sea cucumber Stichopus monotuberculatus.
2015,
Pubmed
,
Echinobase