Isolation and Identification of Cryptic Bioactive Regions in Bovine Achilles Tendon Collagen

Banerjee, Pradipta; Suseela, G.; Shanthi, C.

doi:10.1007/s10930-012-9415-8

Cited by 23 publications

(10 citation statements)

References 53 publications

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“…The CH samples were assayed for their lipid peroxidation inhibition activity in accordance with previous reports (Banerjee, Suseela, & Shanthi, ). The methodology used, in brief, is as follows: Equal volumes of 50 mM linolenic acid in absolute ethanol and CH sample in phosphate buffer (concentration used: 1 mg/ml) were mixed.…”

Section: Methodsmentioning

confidence: 99%

Utilization of marine industry waste derived collagen hydrolysate as peroxide inhibition agents in lipid‐based food

Das

Dey

Chakraborty

et al. 2017

J Food Process Preserv

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Marine industry waste is rich in the extracellular structural protein collagen, excised fragments of which are known to display numerous physiological activities. This study aims at screening waste derived collagen hydrolysates for their utility as peroxide inhibitors in lipid‐based food and cytoprotective agents via cell culture. Collagen was isolated from Pacu and Rohu waste by acid dissolution and salt precipitation. The purified collagen samples were analyzed through electrophoresis, spectral, and elution pattern and confirmed to be of Type‐I. The hydrolysates exhibited a molecular weight around 5 kDa and were found to be in random conformation. The hydrolysates substantially decreased peroxidation levels by 80–90% in linoleic acid model and were equally effective in market available products: cod liver oil and mustard oil. Cell culture assays showed that the hydrolysates were not toxic and capable of increasing cell survival rate by scavenging lipid peroxides generated in situ. Practical applications Peroxidation of lipid‐based food products leads to decreased quality, low benefit‐to‐cost ratio, and imparts harmful effects on consumption, thus requiring synthetic antioxidants to be added to the food. Synthetic oxidation inhibitors currently used carry the risk of carcinogenicity, making the search for natural, nontoxic, and biocompatible peroxide inhibitors a research hotspot. Collagen hydrolysates are bioactive, nontoxic, immune‐compatible, provide added nutritional benefits on consumption and as seen in this study, can be mass isolated from marine industrial wastes making them the perfect functional food additive to be replacing synthetic antioxidants. The utilization of waste would reduce pollution, add substantial value to a common industrial waste and remove the cost of peroxide inhibitor synthesis leading to decrease in the food price and increased shelf life.

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Section: Methodsmentioning

confidence: 99%

Utilization of marine industry waste derived collagen hydrolysate as peroxide inhibition agents in lipid‐based food

Das

Dey

Chakraborty

et al. 2017

J Food Process Preserv

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“…Collagen hydrolysis was done according to the protocol described in an earlier work (Banerjee et al 2012). Briefly, crude protease was obtained from Alcaligenes odorans and incubated for 24 h with bovine tendon collagen suspended in slightly alkaline buffer at 37°C.…”

Section: Initial Separation Of the Peptidesmentioning

confidence: 99%

“…The fraction E was resolved as reported earlier (Banerjee et al 2012) by running through sephadex G100 column into three peptide fractions, E1, E2, and E2b, as displayed in Fig. 2a.…”

Section: Purification Of the Active Cryptic Peptidesmentioning

confidence: 99%

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Screening for novel cell adhesive regions in bovine Achilles tendon collagen peptides

Banerjee

Mehta

Shanthi

2014

Biochem. Cell Biol.

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Collagen, a major structural protein of the ECM, is known for its high cell adherence capacity. This study was conducted to identify regions in collagen that harbour such bioactivity. Collagen from tendon was hydrolysed and the peptides fractionated using ion-exchange chromatography (IEC). Isolated peptide fractions were coated onto disposable dishes and screened for cell adherence and proliferative abilities. Active IEC fractions were further purified by chromatography, and two peptides, C2 and E1 with cell adhesion ability, were isolated. A cell adhesion assay done with different amounts of C2 coated onto disposable dishes revealed the maximum adhesion to be 94.6%, compared with 80% for collagen coated dishes and an optimum peptide coating density of 0.507 nmoles per cm(2) area of the dish. Growth of cells on C2, collagen, and E1 revealed a similar pattern and a reduction in the doubling time compared with cells grown on uncoated dishes. C2 had a mass of 2.046 kDa with 22 residues, and sequence analysis revealed a higher percentage occurrence of hydrophilic residues compared with other regions in collagen. Docking studies revealed GDDGEA in C2 as the probable site of interaction with integrins α2β1 and α1β1, and stability studies proved C2 to be mostly protease-resistant.

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“…: high-pressure membrane technologies) or are difficult to scale up (ex. : chromatographic techniques) [16][17][18][19]. In that way, one approach that can be considered for separating such compounds is liquid-liquid extraction using aqueous two-phase systems (ATPS).…”

Section: Introductionmentioning

confidence: 99%

Recovery of casein-derived peptides with in vitro inhibitory activity of angiotensin converting enzyme (ACE) using aqueous two-phase systems

Souza

Coimbra

Oliveira

et al. 2014

Journal of Chromatography B

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Peptides inhibiting the activity of angiotensin converting enzyme (ACE) were obtained by trypsin-catalyzed hydrolysis of bovine milk casein, performed at 37°C, during 1, 2, 5, 8 and 24h. Results of in vitro inhibitory activity ranged between 13.4% and 78.5%. The highest ACE inhibitory activity was evidenced for hydrolysates obtained after 2h of reaction. Aqueous two-phase systems (ATPS) formed by polyethylene glycol of 1500gmol (PEG 1500)+sodium phosphate or potassium phosphates were produced and evaluated, in terms of partition coefficients (K) and extraction yields (y), to recovery the casein hydrolysates at room temperature. In ATPS containing sodium phosphate, the peptides showed a slightly greater affinity toward the bottom salt-rich phase (0.1≤K≤0.9; 5.7%≤y≤47%). In the case of ATPS containing potassium phosphates, these molecules showed substantially greater affinity toward the top polymer-rich phase (137≤K≤266; y≥99%). These results point out extraction using PEG 1500/potassium phosphate ATPS is an efficient technique to recover casein hydrolysates containing ACE inhibitors peptides. Outlined data will be helpful in integrating such unit operation to larger scale processes.

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Isolation and Identification of Cryptic Bioactive Regions in Bovine Achilles Tendon Collagen

Cited by 23 publications

References 53 publications

Utilization of marine industry waste derived collagen hydrolysate as peroxide inhibition agents in lipid‐based food

Utilization of marine industry waste derived collagen hydrolysate as peroxide inhibition agents in lipid‐based food

Screening for novel cell adhesive regions in bovine Achilles tendon collagen peptides

Recovery of casein-derived peptides with in vitro inhibitory activity of angiotensin converting enzyme (ACE) using aqueous two-phase systems

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