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Titre du document / Document title

Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR

Auteur(s) / Author(s)

MATSUI Toshiro (1) ; YUKIYOSHI Akiko (1) ; DOI Shima (2) ; SUGIMOTO Hiroyuki (2) ; YAMADA Hideo (2) ; MATSUMOTO Kiyoshi (1) ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

(1) Division of Bioresources and Biosciences, Faculty of Agriculture, Graduate School, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, JAPON
(2) Yamada Apiculture Center, Inc., Ichiba 194, Kagamino-Cho, Tomada-Gun, Okayama 708-0393, JAPON

Résumé / Abstract

In order to clarify the potential physiological function of royal jelly (RJ), we report here the gastrointestinal enzyme production of antihypertensive peptides from RJ. Intact RJ and its protein fraction did not retard the action of angiotensin I-converting enzyme (ACE) activity at all. However, development of ACE inhibition power of RJ was newly observed by pepsin hydrolysis (IC50=0.358 mg protein/mL), and the subsequent trypsin and chymotrypsin hydrolyses (IC50=0.099 mg protein/mL). Single oral administration of this gastrointestinal RJ hydrolysate (1 glkg dose) in 10-week spontaneously hypertensive rat resulted in a significant reduction of systolic blood pressure of 22.7 ± 3.6 mmHg at 2 hr (P<0.05 vs. 0 hr by one-way ANOVA, n=7). Then, the RJ hydrolysate was fractionated with gel permeation chromatography to obtain the di- and tri-peptides (DTP) fraction. As a result of isolation from the DTP fraction by reversed phase-high performance liquid chromatography, eleven ACE inhibitory peptides were isolated from the DTP-RJ hydrolysate. Some of the ACE inhibitors were derived from the RJ-glycoprotein; eight peptides with the IC50 value of <10 μM were identified from natural resources for the first time. Consequently, RJ protein was thought to be a good resource of ACE inhibitory peptides produced by the gastrointestinal enzyme hydrolyses.

Revue / Journal Title

Journal of nutritional biochemistry    ISSN  0955-2863 

Source / Source

2002, vol. 13, no2, pp. 80-86 (32 ref.)

Langue / Language

Anglais

Editeur / Publisher

Elsevier, New York, NY, ETATS-UNIS  (1990) (Revue)

Mots-clés anglais / English Keywords

Invertebrata

;

Arthropoda

;

Insecta

;

Hymenoptera

;

Aculeata

;

Apoidea

;

Apidae

;

Vertebrata

;

Mammalia

;

Rodentia

;

Social insect

;

Cardiovascular disease

;

Feeding

;

Enzyme

;

Hydrolases

;

Peptidases

;

Peptidyl-dipeptidases

;

Apis mellifera

;

Animal

;

Rat

;

Pharmacognosy

;

Antihypertensive agent

;

Digestive system

;

Hydrolysis

;

Hypertension

;

Peptidyl-dipeptidase A

;

Inhibition

;

Supplemented diet

;

Royal jelly

;

Protein

;

Peptides

;

Biological activity

;

Mots-clés français / French Keywords

Invertebrata

;

Arthropoda

;

Insecta

;

Hymenoptera

;

Aculeata

;

Apoidea

;

Apidae

;

Vertebrata

;

Mammalia

;

Rodentia

;

Insecte social

;

Appareil circulatoire pathologie

;

Alimentation

;

Enzyme

;

Hydrolases

;

Peptidases

;

Peptidyl-dipeptidases

;

Apis mellifera

;

Animal

;

Rat

;

Pharmacognosie

;

Antihypertenseur

;

Appareil digestif

;

Hydrolyse

;

Hypertension artérielle

;

Peptidyl-dipeptidase A

;

Inhibition

;

Régime alimentaire enrichi

;

Gelée royale

;

Protéine

;

Peptide

;

Activité biologique

;

Mots-clés espagnols / Spanish Keywords

Invertebrata

;

Arthropoda

;

Insecta

;

Hymenoptera

;

Aculeata

;

Apoidea

;

Apidae

;

Vertebrata

;

Mammalia

;

Rodentia

;

Insecto social

;

Aparato circulatorio patología

;

Alimentación

;

Enzima

;

Hydrolases

;

Peptidases

;

Peptidyl-dipeptidases

;

Apis mellifera

;

Animal

;

Rata

;

Farmacognosia

;

Antihipertensivo

;

Aparato digestivo

;

Hidrólisis

;

Hipertensión arterial

;

Peptidyl-dipeptidase A

;

Inhibición

;

Régimen alimenticio enriquecido

;

Jalea real

;

Proteína

;

Péptido

;

Actividad biológica

;

Localisation / Location

INIST-CNRS, Cote INIST : 15374, 35400010024363.0030

Nº notice refdoc (ud4) : 13483078



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