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Tytuł pozycji:

Protease Inhibitors Purified from the Canola Meal Extracts of Two Genetically Diverse Genotypes Exhibit Antidiabetic and Antihypertension Properties.

Tytuł:
Protease Inhibitors Purified from the Canola Meal Extracts of Two Genetically Diverse Genotypes Exhibit Antidiabetic and Antihypertension Properties.
Autorzy:
Hussain S; Graham Centre (an Alliance between Charles Sturt University and the NSW Department of Primary Industries), Boorooma Street, Wagga Wagga, NSW 2678, Australia.; ARC Industrial Transformation Training Centre for Functional Grains, School of Biomedical Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, NSW 2678, Australia.
Rehman AU; Graham Centre (an Alliance between Charles Sturt University and the NSW Department of Primary Industries), Boorooma Street, Wagga Wagga, NSW 2678, Australia.; ARC Industrial Transformation Training Centre for Functional Grains, School of Biomedical Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, NSW 2678, Australia.
Luckett DJ; Graham Centre (an Alliance between Charles Sturt University and the NSW Department of Primary Industries), Boorooma Street, Wagga Wagga, NSW 2678, Australia.
Naqvi SMS; Graham Centre (an Alliance between Charles Sturt University and the NSW Department of Primary Industries), Boorooma Street, Wagga Wagga, NSW 2678, Australia.
Blanchard CL; Graham Centre (an Alliance between Charles Sturt University and the NSW Department of Primary Industries), Boorooma Street, Wagga Wagga, NSW 2678, Australia.; ARC Industrial Transformation Training Centre for Functional Grains, School of Biomedical Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, NSW 2678, Australia.
Źródło:
Molecules (Basel, Switzerland) [Molecules] 2021 Apr 04; Vol. 26 (7). Date of Electronic Publication: 2021 Apr 04.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Original Publication: Basel, Switzerland : MDPI, c1995-
MeSH Terms:
Antihypertensive Agents/*pharmacology
Brassica napus/*chemistry
Dipeptidyl Peptidase 4/*chemistry
Enzyme Inhibitors/*pharmacology
Hypoglycemic Agents/*pharmacology
Peptidyl-Dipeptidase A/*chemistry
Amino Acid Sequence ; Antihypertensive Agents/chemistry ; Antihypertensive Agents/isolation & purification ; Brassica napus/genetics ; Brassica napus/metabolism ; Dipeptidyl Peptidase 4/metabolism ; Enzyme Assays ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/isolation & purification ; Genotype ; Humans ; Hypoglycemic Agents/chemistry ; Hypoglycemic Agents/isolation & purification ; Isoelectric Focusing ; Kinetics ; Liquid-Liquid Extraction/methods ; Peptidyl-Dipeptidase A/metabolism ; Plant Extracts/chemistry
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Grant Information:
Tri-Faculty Open Access Publishing Scheme Charles Sturt University
Contributed Indexing:
Keywords: angiotensin converting enzyme; canola meal; dipeptidyl peptidase-IV; protease inhibitor
Substance Nomenclature:
0 (Antihypertensive Agents)
0 (Enzyme Inhibitors)
0 (Hypoglycemic Agents)
0 (Plant Extracts)
EC 3.4.14.5 (Dipeptidyl Peptidase 4)
EC 3.4.15.1 (ACE protein, human)
EC 3.4.15.1 (Peptidyl-Dipeptidase A)
Entry Date(s):
Date Created: 20210430 Date Completed: 20210517 Latest Revision: 20210517
Update Code:
20240104
PubMed Central ID:
PMC8038563
DOI:
10.3390/molecules26072078
PMID:
33916639
Czasopismo naukowe
Valorization of vegetable oil waste residues is gaining importance due to their high protein and polyphenol contents. Protease inhibitors (PIs), proteins from these abundantly available waste residues, have recently gained importance in treating chronic diseases. This research aimed to use canola meal of genetically diverse Brassica napus genotypes, BLN-3347 and Rivette, to identify PIs with diverse functionalities in therapeutic and pharmacological applications. The canola meal PI purification steps involved: native PAGE and trypsin inhibition activity, followed by ammonium sulfate fractionation, anion exchange, gel filtration, and reverse-phase chromatography. The purified PI preparations were characterized using SDS-PAGE, isoelectric focusing (IEF), and N terminal sequencing. SDS-PAGE analysis of PI preparations under native reducing and nonreducing conditions revealed three polymorphic PIs in each genotype. The corresponding IEF of the genotype BLN-3347, exhibited three acidic isoforms with isoelectric points (p I ) of 4.6, 4.0, and 3.9, while Rivette possessed three isoforms, exhibiting two basic forms of p I 8.65 and 9.9, and one acidic of p I 6.55. Purified PI preparations from both the genotypes displayed dipeptidyl peptidase-IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibition activities; the BLN-3347 PI preparation exhibited a strong inhibitory effect with lower IC 50 values (DPP-IV 37.42 µg/mL; ACE 129 µg/mL) than that from Rivette (DPP-IV 67.97 µg/mL; ACE 376.2 µg/mL). In addition to potential human therapy, these highly polymorphic PIs, which can inhibit damaging serine proteases secreted by canola plant pathogens, have the potential to be used by canola plant breeders to seek qualitative trait locus (QTLs) linked to genes conferring resistance to canola diseases.

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