The Experts below are selected from a list of 303 Experts worldwide ranked by ideXlab platform
Richard J. Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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milk protein hydrolysates activate 5 ht2c serotonin receptors influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (<1 kDa), were hydrophobic in nature and had a pI between 8.6 and 13.2. These different physicochemical characteristics together with the stability of NaCNH-240 min to simulated intestinal digestion, allow prediction of a favourable outcome regarding the bioavailability of the bioactive peptides therein. These results reinforce the potential of milk-derived bioactive peptides to be developed into functional foods targeted at 5-HT2C receptor modulation.
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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (
Paul M. Cino - One of the best experts on this subject based on the ideXlab platform.
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Improvement of sordarin production through process optimization: combining traditional approaches with DOE
Journal of Industrial Microbiology & Biotechnology, 2007Co-Authors: Thomas P Tully, Steven R. Schwarz, Susan C. Durand, Jeffrey M. Howell, Ramesh N Patel, James S. Bergum, Paul M. CinoAbstract:BMS-353645, also known as sordarin, was of interest based on its activity against pathogenic fungi. The objective of these studies was to provide high quality Starting Substrate for chemical modification aimed at further improving biological activity, with particular interest in the inhibition of Aspergillus . In the work presented here, Design of Experiments, or DOE, was successfully combined with traditional approaches to significantly improve sordarin yields in fermentation flasks. Overall, yields were increased 25-fold from
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Improvement of sordarin production through process optimization: combining traditional approaches with DOE
Journal of Industrial Microbiology & Biotechnology, 2007Co-Authors: Thomas P Tully, Steven R. Schwarz, Susan C. Durand, Jeffrey M. Howell, Ramesh N Patel, James S. Bergum, Paul M. CinoAbstract:BMS-353645, also known as sordarin, was of interest based on its activity against pathogenic fungi. The objective of these studies was to provide high quality Starting Substrate for chemical modification aimed at further improving biological activity, with particular interest in the inhibition of Aspergillus . In the work presented here, Design of Experiments, or DOE, was successfully combined with traditional approaches to significantly improve sordarin yields in fermentation flasks. Overall, yields were increased 25-fold from
Sarah E Oconnor - One of the best experts on this subject based on the ideXlab platform.
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aza tryptamine Substrates in monoterpene indole alkaloid biosynthesis
Chemistry & Biology, 2009Co-Authors: Hyangyeol Lee, Nancy Yerkes, Sarah E OconnorAbstract:Biosynthetic pathways can be hijacked to yield novel compounds by introduction of novel Starting materials. Here we have altered tryptamine, which serves as the Starting Substrate for a variety of alkaloid biosynthetic pathways, by replacing the indole with one of four aza-indole isomers. We show that two aza-tryptamine Substrates can be successfully incorporated into the products of the monoterpene indole alkaloid pathway in Catharanthus roseus. Use of unnatural heterocycles in precursor-directed biosynthesis, in both microbial and plant natural product pathways, has not been widely demonstrated, and successful incorporation of Starting Substrate analogs containing the aza-indole functionality has not been previously reported. This work serves as a Starting point to explore fermentation of aza-alkaloids from other tryptophan- and tryptamine-derived natural product pathways.
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silencing of tryptamine biosynthesis for production of nonnatural alkaloids in plant culture
Proceedings of the National Academy of Sciences of the United States of America, 2009Co-Authors: Weerawat Runguphan, Justin J Maresh, Sarah E OconnorAbstract:Natural products have long served as both a source and inspiration for pharmaceuticals. Modifying the structure of a natural product often improves the biological activity of the compound. Metabolic engineering strategies to ferment "unnatural" products have been enormously successful in microbial organisms. However, despite the importance of plant derived natural products, metabolic engineering strategies to yield unnatural products from complex, lengthy plant pathways have not been widely explored. Here, we show that RNA mediated suppression of tryptamine biosynthesis in Catharanthus roseus hairy root culture eliminates all production of monoterpene indole alkaloids, a class of natural products derived from two Starting Substrates, tryptamine and secologanin. To exploit this chemically silent background, we introduced an unnatural tryptamine analog to the production media and demonstrated that the silenced plant culture could produce a variety of novel products derived from this unnatural Starting Substrate. The novel alkaloids were not contaminated by the presence of the natural alkaloids normally present in C. roseus. Suppression of tryptamine biosynthesis therefore did not appear to adversely affect expression of downstream biosynthetic enzymes. Targeted suppression of Substrate biosynthesis therefore appears to be a viable strategy for programming a plant alkaloid pathway to more effectively produce desirable unnatural products. Moreover, although tryptamine is widely found among plants, this silenced line demonstrates that tryptamine does not play an essential role in growth or development in C. roseus root culture. Silencing the biosynthesis of an early Starting Substrate enhances our ability to harness the rich diversity of plant based natural products.
Alice B. Nongonierma - One of the best experts on this subject based on the ideXlab platform.
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milk protein hydrolysates activate 5 ht2c serotonin receptors influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (<1 kDa), were hydrophobic in nature and had a pI between 8.6 and 13.2. These different physicochemical characteristics together with the stability of NaCNH-240 min to simulated intestinal digestion, allow prediction of a favourable outcome regarding the bioavailability of the bioactive peptides therein. These results reinforce the potential of milk-derived bioactive peptides to be developed into functional foods targeted at 5-HT2C receptor modulation.
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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (
Timothy G. Dinan - One of the best experts on this subject based on the ideXlab platform.
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selective enrichment of dairy phospholipids in a buttermilk Substrate through investigation of enzymatic hydrolysis of milk proteins in conjunction with ultrafiltration
International Dairy Journal, 2017Co-Authors: Timothy G. Dinan, Kate M Barry, Philip M KellyAbstract:Abstract Extensive enzymatic hydrolysis of milk proteins in reconstituted buttermilk powder was combined with ultrafiltration to generate a phospholipid (PL) enriched fraction with maximum permeation of hydrolysed peptides. Buttermilk, naturally high in PLs, is the ideal Substrate for enrichment of these bio- and techno-functionally active compounds. A 7.8 fold increase in PL was achieved in the 50 kDa retentate; 6.16 ± 0.02% total PL compared with 0.79 ± 0.01% in the Starting Substrate, an increase considerably greater than previously reported. Total lipid content (% dry matter) increased 6.3 fold in the retentate, 43.43 ± 0.61%, from the Starting Substrate, 6.84 ± 0.17%. This combined strategic approach enabled maximum enrichment of PLs with no transmission of lipid material into the permeate, 0.09 ± 0.02% total lipid, and non-detectable levels of PLs recovered in the permeate, 0.00 ± 0.01% total PL.
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milk protein hydrolysates activate 5 ht2c serotonin receptors influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (<1 kDa), were hydrophobic in nature and had a pI between 8.6 and 13.2. These different physicochemical characteristics together with the stability of NaCNH-240 min to simulated intestinal digestion, allow prediction of a favourable outcome regarding the bioavailability of the bioactive peptides therein. These results reinforce the potential of milk-derived bioactive peptides to be developed into functional foods targeted at 5-HT2C receptor modulation.
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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the Starting Substrate and isolation of bioactive fractions
Food & Function, 2013Co-Authors: Alice B. Nongonierma, Harriët Schellekens, Timothy G. Dinan, John F. Cryan, Richard J. FitzgeraldAbstract:Milk protein hydrolysates generated with different Starting Substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only Starting Substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semi-preparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (
