Undergraduate Thesis Or Project

 

Inhibition of pancreatic lipase by grape seed and tea extracts and their primary catechins in vitro Public Deposited

https://ir.library.oregonstate.edu/concern/undergraduate_thesis_or_projects/47429b65r

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  • Inhibiting pancreatic lipase activity is an effective means of reducing fat absorption, which may have a role in combating obesity by limiting energy intake. The use of pharmaceutical lipase inhibitors has been limited due to the prevalence of undesirable side effects. Polyphenols represent an alternative strategy to inhibit digestive enzymes using safe, gentle, and cost-effective extracts derived from plant sources. Thus, this study evaluated alternative options by testing various polyphenol-rich plant extracts (grape seed, green tea, TeaVigo®, and white tea) for their ability to inhibit pancreatic lipase activity. Using an in vitro fluorescence assay, the relative potency of extracts tested was determined in comparison to the pharmaceutical orlistat. In addition, the most abundant catechins found in these extracts, epicatechin gallate (ECG), epigallocatechin (EGC), and epigallocatechin gallate (EGCG), were also tested for the ability to inhibit pancreatic lipase. Results showed the most effective plant-based lipase inhibitors were the concentrated green tea product, TeaVigo® and green tea. Results with the individual catechin trials showed EGCG and EGC were the most potent lipase inhibitors in the plant extracts.
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  • This work was funded by a grant from Oregon State Unversity’s URSA-Engage Program and generous support from USANA Health Sciences, Inc. (Salt Lake City, Utah, USA)
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  • Created using Microsoft PowerPoint 2010. Converted to pdf using Acrobat 6.
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  • description.provenance : Made available in DSpace on 2014-05-19T14:04:29Z (GMT). No. of bitstreams: 3 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) Hess_M_Lipase Poster_AM_Final.pptx: 346282 bytes, checksum: b93da199e3f7036b10876134b308a08f (MD5) Hess_M_Lipase Poster_Final.pdf: 324631 bytes, checksum: 85b4f4dbece52a2fd2bcd13abc6b0356 (MD5)
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2014-05-19T14:04:29Z (GMT) No. of bitstreams: 3 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) Hess_M_Lipase Poster_AM_Final.pptx: 346282 bytes, checksum: b93da199e3f7036b10876134b308a08f (MD5) Hess_M_Lipase Poster_Final.pdf: 324631 bytes, checksum: 85b4f4dbece52a2fd2bcd13abc6b0356 (MD5)
  • description.provenance : Submitted by Michelle Hess (hessmic@onid.oregonstate.edu) on 2014-05-19T01:08:57Z No. of bitstreams: 3 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) Hess_M_Lipase Poster_AM_Final.pptx: 346282 bytes, checksum: b93da199e3f7036b10876134b308a08f (MD5) Hess_M_Lipase Poster_Final.pdf: 324631 bytes, checksum: 85b4f4dbece52a2fd2bcd13abc6b0356 (MD5)

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