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H L Bruce - One of the best experts on this subject based on the ideXlab platform.
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pretreatment with formic acid enhances the production of small peptides from highly cross linked collagen of Spent Hens
Food Chemistry, 2018Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, H L BruceAbstract:Abstract Small collagen peptides are associated with various benefits, such as bone and skin health. However, preparation of small collagen peptides from terrestrial vertebrate origins remains a challenge. Here, we show that pretreatment with formic acid enhanced the production of small collagen peptides from Spent hen skin. After pretreatment with formic acid, the percentage of small peptides below 2 kDa increased to 48.92% and 43.34% from 33.79% and 36.32% for heat-soluble collagen (HSC) and pepsin-soluble collagen (PSC), respectively. Pretreatment with formic acid degraded telopeptides and released the cross-links (pyrrole and pyridinoline), which made hen collagen more susceptible to papain hydrolysis. LC-MS/MS results revealed that none of the peptides identified from HSC-FA (formic acid)-Papain and PSC-FA-Papain were derived from cross-linked telopeptides. These results demonstrated that formic acid assisted the hydrolysis of highly cross-linked collagen of Spent Hens, and it might also be used to produce small collagen peptides from other aged, vertebrate collagens.
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removing cross linked telopeptides enhances the production of low molecular weight collagen peptides from Spent Hens
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, H L BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (<1.4 kDa) that were obtained from pepsin-soluble collagen increased to 32.59% compared to heat-soluble collagen peptides (16.10%). Fourier transform infrared spectroscopy results indicated that telopeptide cleavage retained the triple-helical conformation of collagen. Liquid chromatography–tandem mass spectrometry analysis suggested that Gly-X-Y (X is often proline, while Y is either hydroxyproline or hydroxylysine) repeats were not the main factors that hindered the enzymatic hydrolysis of collagen molecules. However, cross-link quantification demonstrated that trivalent ...
Hui Hong - One of the best experts on this subject based on the ideXlab platform.
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pretreatment with formic acid enhances the production of small peptides from highly cross linked collagen of Spent Hens
Food Chemistry, 2018Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, H L BruceAbstract:Abstract Small collagen peptides are associated with various benefits, such as bone and skin health. However, preparation of small collagen peptides from terrestrial vertebrate origins remains a challenge. Here, we show that pretreatment with formic acid enhanced the production of small collagen peptides from Spent hen skin. After pretreatment with formic acid, the percentage of small peptides below 2 kDa increased to 48.92% and 43.34% from 33.79% and 36.32% for heat-soluble collagen (HSC) and pepsin-soluble collagen (PSC), respectively. Pretreatment with formic acid degraded telopeptides and released the cross-links (pyrrole and pyridinoline), which made hen collagen more susceptible to papain hydrolysis. LC-MS/MS results revealed that none of the peptides identified from HSC-FA (formic acid)-Papain and PSC-FA-Papain were derived from cross-linked telopeptides. These results demonstrated that formic acid assisted the hydrolysis of highly cross-linked collagen of Spent Hens, and it might also be used to produce small collagen peptides from other aged, vertebrate collagens.
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removing cross linked telopeptides enhances the production of low molecular weight collagen peptides from Spent Hens
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, H L BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (<1.4 kDa) that were obtained from pepsin-soluble collagen increased to 32.59% compared to heat-soluble collagen peptides (16.10%). Fourier transform infrared spectroscopy results indicated that telopeptide cleavage retained the triple-helical conformation of collagen. Liquid chromatography–tandem mass spectrometry analysis suggested that Gly-X-Y (X is often proline, while Y is either hydroxyproline or hydroxylysine) repeats were not the main factors that hindered the enzymatic hydrolysis of collagen molecules. However, cross-link quantification demonstrated that trivalent ...
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Removing Cross-Linked Telopeptides Enhances the Production of Low-Molecular-Weight Collagen Peptides from Spent Hens
2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, Heather L. BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (
Meram Chalamaiah - One of the best experts on this subject based on the ideXlab platform.
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pretreatment with formic acid enhances the production of small peptides from highly cross linked collagen of Spent Hens
Food Chemistry, 2018Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, H L BruceAbstract:Abstract Small collagen peptides are associated with various benefits, such as bone and skin health. However, preparation of small collagen peptides from terrestrial vertebrate origins remains a challenge. Here, we show that pretreatment with formic acid enhanced the production of small collagen peptides from Spent hen skin. After pretreatment with formic acid, the percentage of small peptides below 2 kDa increased to 48.92% and 43.34% from 33.79% and 36.32% for heat-soluble collagen (HSC) and pepsin-soluble collagen (PSC), respectively. Pretreatment with formic acid degraded telopeptides and released the cross-links (pyrrole and pyridinoline), which made hen collagen more susceptible to papain hydrolysis. LC-MS/MS results revealed that none of the peptides identified from HSC-FA (formic acid)-Papain and PSC-FA-Papain were derived from cross-linked telopeptides. These results demonstrated that formic acid assisted the hydrolysis of highly cross-linked collagen of Spent Hens, and it might also be used to produce small collagen peptides from other aged, vertebrate collagens.
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removing cross linked telopeptides enhances the production of low molecular weight collagen peptides from Spent Hens
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, H L BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (<1.4 kDa) that were obtained from pepsin-soluble collagen increased to 32.59% compared to heat-soluble collagen peptides (16.10%). Fourier transform infrared spectroscopy results indicated that telopeptide cleavage retained the triple-helical conformation of collagen. Liquid chromatography–tandem mass spectrometry analysis suggested that Gly-X-Y (X is often proline, while Y is either hydroxyproline or hydroxylysine) repeats were not the main factors that hindered the enzymatic hydrolysis of collagen molecules. However, cross-link quantification demonstrated that trivalent ...
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Removing Cross-Linked Telopeptides Enhances the Production of Low-Molecular-Weight Collagen Peptides from Spent Hens
2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, Heather L. BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (
Bimol C Roy - One of the best experts on this subject based on the ideXlab platform.
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pretreatment with formic acid enhances the production of small peptides from highly cross linked collagen of Spent Hens
Food Chemistry, 2018Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, H L BruceAbstract:Abstract Small collagen peptides are associated with various benefits, such as bone and skin health. However, preparation of small collagen peptides from terrestrial vertebrate origins remains a challenge. Here, we show that pretreatment with formic acid enhanced the production of small collagen peptides from Spent hen skin. After pretreatment with formic acid, the percentage of small peptides below 2 kDa increased to 48.92% and 43.34% from 33.79% and 36.32% for heat-soluble collagen (HSC) and pepsin-soluble collagen (PSC), respectively. Pretreatment with formic acid degraded telopeptides and released the cross-links (pyrrole and pyridinoline), which made hen collagen more susceptible to papain hydrolysis. LC-MS/MS results revealed that none of the peptides identified from HSC-FA (formic acid)-Papain and PSC-FA-Papain were derived from cross-linked telopeptides. These results demonstrated that formic acid assisted the hydrolysis of highly cross-linked collagen of Spent Hens, and it might also be used to produce small collagen peptides from other aged, vertebrate collagens.
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removing cross linked telopeptides enhances the production of low molecular weight collagen peptides from Spent Hens
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, H L BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (<1.4 kDa) that were obtained from pepsin-soluble collagen increased to 32.59% compared to heat-soluble collagen peptides (16.10%). Fourier transform infrared spectroscopy results indicated that telopeptide cleavage retained the triple-helical conformation of collagen. Liquid chromatography–tandem mass spectrometry analysis suggested that Gly-X-Y (X is often proline, while Y is either hydroxyproline or hydroxylysine) repeats were not the main factors that hindered the enzymatic hydrolysis of collagen molecules. However, cross-link quantification demonstrated that trivalent ...
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Removing Cross-Linked Telopeptides Enhances the Production of Low-Molecular-Weight Collagen Peptides from Spent Hens
2017Co-Authors: Hui Hong, Bimol C Roy, Meram Chalamaiah, Shreyak Chaplot, Heather L. BruceAbstract:The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (
Aman Ullah - One of the best experts on this subject based on the ideXlab platform.
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lipid derived hybrid bionanocomposites from Spent Hens
Materials today communications, 2020Co-Authors: Muhammad Safder, Feral Temelli, Aman UllahAbstract:Abstract A monomer was synthesized using the mixture of fatty acids obtained through the hydrolysis of triglycerides extracted from Spent Hens. The reaction conditions of temperature and time were studied to obtain a high molecular weight biopolymer using bulk polymerization. The bionanocomposites were then prepared with different ratios of nanoclay (0, 3, 5, and 10 %) addition using in situ polymerization. The bionanocomposite films were prepared using compression molding and the effect of nanoparticle addition, in terms of their dispersion, was investigated by different characterization techniques. Results showed enhanced thermal stability for nanoreinforced biocomposites. The flammability test showed substantial improvements in the flame retardancy of bionanocomposites compared to the neat homopolymer. These findings suggest that high-performance bionanomaterials can be prepared from Spent hen lipids through in situ addition of nanoclay during polymerization.
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supercritical co2 extraction and solvent free rapid alternative bioepoxy production from Spent Hens
Journal of CO 2 Utilization, 2019Co-Authors: Muhammad Safder, Feral Temelli, Aman UllahAbstract:Abstract Spent Hens are by-product of egg and hatching egg production and a potential source of renewable compounds. In this study, lipids were extracted using supercritical carbon dioxide (SC−CO2) at 50 − 70 °C, 30 − 50 MPa, and constant CO2 flow rate of 1 L/min. The maximum yield of total lipid 37 ± 0.4 % (w/w) with 91.4% recovery was obtained at 50 MPa/70 °C. Fatty acid compositional analysis was performed using gas chromatography with flame ionization detector (GC-FID). Helium ion microscopy (HIM) was used to assess the morphological changes before and after extraction. Furthermore, epoxidation of the extracted lipids was conducted with and without the use of a solvent, where the solvent-free epoxidation was completed within 20 min and the yield was comparable. The reaction progress was monitored by attenuated total reflectance-Fourier transform infrared (ATR-FTIR) and proton nuclear magnetic resonance (1H NMR) spectroscopy analysis, which showed the conversion rates of 59.8, 84.2 and 100% at 5, 10, and 20 min, respectively. The findings suggest that an alternative bio-epoxy can be produced using SC−CO2 extraction and solvent-free oxidation of extracted lipids from poultry industry waste/by-product.
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Hybrid Bionanocomposites from Spent Hen Proteins
2019Co-Authors: Muhammad Zubair, Aman UllahAbstract:Spent Hens, a poultry by-product, have little economic value for processing and mostly end up in landfills. However, there are concerns over disposal of Spent Hens; therefore, it is pertinent to find out alternative uses that are environmentally sound. On the other hand, single-use plastic packaging is leading to a global environmental crisis. In this study, proteins were extracted from Spent hen, plasticized, and processed into films by compression molding. The hybrid bionanocomposite films were successfully prepared using glycerol as a plasticizer, chitosan as a cross-linker, and varying concentrations of nanoclay as a nanoreinforcement. The effects of nanoreinforcements, plasticization, and cross-linking were then evaluated on thermal, mechanical, and barrier properties of the prepared bionanocomposite films. Various concentrations of nanoclay and chitosan were dispersed in the protein matrix. However, with the same plasticizer loading, the optimum addition of chitosan and nanoclay led to almost twofold increase in the mechanical strength, compared to neat protein films. The results indicated that at optimal conditions, a good intercalation and/or exfoliation of the protein biopolymers into clay interlayer galleries was observed leading to improved thermal, thermomechanical, and barrier properties. These hybrid bionanocomposite films have great future potential to be used in packaging and other applications
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extraction optimization and characterization of lipids from Spent Hens an unexploited sustainable bioresource
Journal of Cleaner Production, 2019Co-Authors: Muhammad Safder, Feral Temelli, Aman UllahAbstract:Abstract Spent hen, a poultry industry by-product with little market value and high lipid content, can be used as a new and sustainable biomass source for lipid production. This study focused on conventional extraction methods and compared them with the microwave-assisted extraction of lipids from the Spent hen. Over 95% of the lipids were recovered within 10 min using microwaves. Factors affecting the extraction conditions, including extraction time, temperature, and the solvent-to-feed ratio on the lipid extraction yield were studied using response surface methodology. To account for the low sample size, parametric bootstrapping was used with a replacement approach. Data in all combinations were bootstrapped 10,000 times, which showed a decrease in standard deviation. Fatty acid profiles of extracts obtained in different conditions were investigated using gas chromatography equipped with mass spectrometry and a flame ionization detector for qualitative and quantitative analysis, respectively. The lipids predominantly contained oleic (46%), linoleic (∼22%), and palmitic (∼23%) acids. Proton nuclear magnetic spectroscopy and Fourier transform infrared spectroscopy were used to characterize different functional groups in the lipids. The phase transitions and thermal degradation behavior of lipids were determined using differential scanning calorimetry and thermogravimetric analysis, respectively.