Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Autor: M Ghorbani, Fidel Toldrá, Alireza Sadeghi Mahoonak, Atefe Maqsoudlou, Hossein Mohebodini, Leticia Mora
Přispěvatelé: Ministry of Science, Research, and Technology (Iran), Ministerio de Economía y Competitividad (España), European Commission
Rok vydání: 2019
Předmět:
Spectrometry
Mass
Electrospray Ionization
Antioxidant
food.ingredient
030309 nutrition & dietetics
DPPH
RJ
medicine.medical_treatment
Angiotensin-Converting Enzyme Inhibitors
Peptide
Mass spectrometry
Ferric Compounds
Antioxidants
03 medical and health sciences
chemistry.chemical_compound
Hydrolysis
0404 agricultural biotechnology
food
Chlorides
Picrates
Antioxidant activity
Tandem Mass Spectrometry
Royal jelly
medicine
Nanotechnology
ACE-inhibitory activity
Subtilisins
Response surface methodology
Chromatography
High Pressure Liquid
Pollen hydrolysate
Bioactive peptides
Plant Proteins
chemistry.chemical_classification
Chromatography
Reverse-Phase
0303 health sciences
Chromatography
Chemistry
Biphenyl Compounds
Fatty Acids
04 agricultural and veterinary sciences
040401 food science
Enzyme
Pollen
Peptides
Oxidation-Reduction
Food Science
Zdroj: Digital.CSIC. Repositorio Institucional del CSIC
instname
Popis: Peptides with a similar antioxidant and ACE-inhibitory activity of royal jelly (RJ) generated from Alcalase hydrolysated pollen (AHP) were predicted by Response Surface Methodology (RSM). The model equations were proposed according to the effects of time and enzyme concentration on the antioxidant and ACE-inhibitory activity. The optimum values for Alcalase concentration and hydrolysis time were 1.5% and 4 h, respectively. Later, AHP was prepared and deproteinised to be further analysed using size-exclusion chromatography (SEC). After SEC separation, fractions with the highest activity of ACE-inhibitory, DPPH radical scavenging and ferric-reducing power were purified by RP-HPLC. The highest ACE-inhibitory and DPPH scavenging activity of fractions was found 100% and 66.61%, respectively. The most active fractions were analysed by nano-liquid chromatography and mass spectrometry in tandem (nLC-MS/MS) and a total of 195 peptide sequences were identified. The origins of all peptides were herbal proteins and certain coincidences with previously described bioactive sequences were discussed.
This work was funded by the Ministry of Science, Research and Technology of Iran and the Grant AGL2014-57367-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness. Ramón y Cajal postdoctoral contract to LM is acknowledged. LC-MS/MS analysis was carried out by in the SCSIE University of Valencia Proteomics Unit (Spain), a member of ISCIII Proteo Red Proteomics Platform.
Databáze: OpenAIRE
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