Matches in SemOpenAlex for { <https://semopenalex.org/work/W3094685150> ?p ?o ?g. }
Showing items 1 to 100 of
100
with 100 items per page.
- W3094685150 endingPage "339" @default.
- W3094685150 startingPage "327" @default.
- W3094685150 abstract "Soy proteins known for their high nutritional value and pronounced techno-functional properties, can be hydrolyzed by using proteolytic enzymes and thus converted into hydrolysates rich in di-, tri- and oligopeptides. The resulting peptides are carriers of valuable biological activities, which make the soy hydrolysates very important in functional food applications as techno-functional and bioactive ingredients. However, commercial incorporation and application of soy protein hydrolysates can be hinderedby their low bioavailability and instability, bitter taste, hygroscopicity and possibility to interact with the food matrix. The aim of this research is encapsulation of the soy protein hydrolysate in liposomes in order to overcome the stated shortcomings, while preserving the biological activities that protein hydrolysates exhibit. The soy hydrolysate was prepared by a two-step enzymatic hydrolysis of a soy protein concentrate using commercial food-grade proteases, endoprotease from Bacillus amyloliquefaciens (Neutrase?) and egzo- and endoprotease from Aspergillus oryzae (Flavourzyme?) and encapsulated within liposomes. The liposomes were produced by a thin film method using a commercial lipid mixture (Phospolipon? 90G) containing mainly phosphatidylcholine. Next, the obtained multilamellar vesicles (MLV) with the soy protein hydrolysate were treated by high-intensity ultrasound waves generated by using (1) an ultrasonic probe at a frequency of 20 kHz and (2) an ultrasonic bath with a frequency 40 kHz. The smallest (310 nm) and uniform (unimodal size distribution) liposomes with the highest efficiency of peptide encapsulation (19 %) were obtained by the probe sonication. The presented results showed that incorporation of the soy protein hydrolysates was achieved within the liposome membrane and caused an increase in the liposome size in all tested formulations, namely: from 297 to 310 nm by using the ultrasonic probe, from 722 to 850 nm by using the ultrasonic bath, while in formulations without the ultrasonic treatments the increase from 2818 to 3464 nm was recorded. The entrapped peptides caused enlargement of all liposomes and the increase in negative charge of zeta potential values, which in the case of MLV liposomes was below -30 mV, indicating high stability of these liposomes. Significant antioxidant activity of the probe-sonicated liposomal formulation was confirmed by the ABTS scavenging ability and iron-chelating activity. Release studies conducted under simulated gastrointestinal conditions confirmed that liposomes provide prolonged release of encapsulated soy protein hydrolysates as compared to diffusion of the free hydrolysate. In the first 75 min, only 20 % of liposome encapsulated soy peptides diffused, which is 2.2-fold lower as compared to the diffusion of the non-encapsulated soy hydrolysate. Liposome encapsulated soy protein hydrolysates may provide the possibility for application in the areas such as food science and technology, with the aim to enhance the nutritional value and shelf life of food products, and develop functional foods." @default.
- W3094685150 created "2020-11-09" @default.
- W3094685150 creator A5030795644 @default.
- W3094685150 creator A5037546583 @default.
- W3094685150 creator A5056131424 @default.
- W3094685150 creator A5085130878 @default.
- W3094685150 creator A5085142504 @default.
- W3094685150 creator A5089917539 @default.
- W3094685150 date "2020-01-01" @default.
- W3094685150 modified "2023-10-16" @default.
- W3094685150 title "Production and characterization of liposomes with encapsulated bioactive soy protein hydrolysate" @default.
- W3094685150 cites W1775749144 @default.
- W3094685150 cites W1780322264 @default.
- W3094685150 cites W1831952493 @default.
- W3094685150 cites W1852812055 @default.
- W3094685150 cites W1971399433 @default.
- W3094685150 cites W1981032124 @default.
- W3094685150 cites W2000311882 @default.
- W3094685150 cites W2024007812 @default.
- W3094685150 cites W2045878301 @default.
- W3094685150 cites W2046201334 @default.
- W3094685150 cites W2089727949 @default.
- W3094685150 cites W2105464438 @default.
- W3094685150 cites W2132409331 @default.
- W3094685150 cites W2162726552 @default.
- W3094685150 cites W2225089390 @default.
- W3094685150 cites W2333922894 @default.
- W3094685150 cites W2467652346 @default.
- W3094685150 cites W2610165180 @default.
- W3094685150 cites W2619508388 @default.
- W3094685150 cites W2883387856 @default.
- W3094685150 cites W2889049588 @default.
- W3094685150 cites W2902059473 @default.
- W3094685150 cites W2923902472 @default.
- W3094685150 doi "https://doi.org/10.2298/hemind200530030p" @default.
- W3094685150 hasPublicationYear "2020" @default.
- W3094685150 type Work @default.
- W3094685150 sameAs 3094685150 @default.
- W3094685150 citedByCount "1" @default.
- W3094685150 countsByYear W30946851502022 @default.
- W3094685150 crossrefType "journal-article" @default.
- W3094685150 hasAuthorship W3094685150A5030795644 @default.
- W3094685150 hasAuthorship W3094685150A5037546583 @default.
- W3094685150 hasAuthorship W3094685150A5056131424 @default.
- W3094685150 hasAuthorship W3094685150A5085130878 @default.
- W3094685150 hasAuthorship W3094685150A5085142504 @default.
- W3094685150 hasAuthorship W3094685150A5089917539 @default.
- W3094685150 hasBestOaLocation W30946851501 @default.
- W3094685150 hasConcept C104628117 @default.
- W3094685150 hasConcept C181199279 @default.
- W3094685150 hasConcept C182220744 @default.
- W3094685150 hasConcept C185154212 @default.
- W3094685150 hasConcept C185592680 @default.
- W3094685150 hasConcept C2777014122 @default.
- W3094685150 hasConcept C2779832904 @default.
- W3094685150 hasConcept C2781204770 @default.
- W3094685150 hasConcept C28800991 @default.
- W3094685150 hasConcept C31903555 @default.
- W3094685150 hasConcept C43617362 @default.
- W3094685150 hasConcept C53270655 @default.
- W3094685150 hasConcept C55493867 @default.
- W3094685150 hasConcept C94412978 @default.
- W3094685150 hasConceptScore W3094685150C104628117 @default.
- W3094685150 hasConceptScore W3094685150C181199279 @default.
- W3094685150 hasConceptScore W3094685150C182220744 @default.
- W3094685150 hasConceptScore W3094685150C185154212 @default.
- W3094685150 hasConceptScore W3094685150C185592680 @default.
- W3094685150 hasConceptScore W3094685150C2777014122 @default.
- W3094685150 hasConceptScore W3094685150C2779832904 @default.
- W3094685150 hasConceptScore W3094685150C2781204770 @default.
- W3094685150 hasConceptScore W3094685150C28800991 @default.
- W3094685150 hasConceptScore W3094685150C31903555 @default.
- W3094685150 hasConceptScore W3094685150C43617362 @default.
- W3094685150 hasConceptScore W3094685150C53270655 @default.
- W3094685150 hasConceptScore W3094685150C55493867 @default.
- W3094685150 hasConceptScore W3094685150C94412978 @default.
- W3094685150 hasFunder F4320322729 @default.
- W3094685150 hasIssue "5" @default.
- W3094685150 hasLocation W30946851501 @default.
- W3094685150 hasLocation W30946851502 @default.
- W3094685150 hasLocation W30946851503 @default.
- W3094685150 hasOpenAccess W3094685150 @default.
- W3094685150 hasPrimaryLocation W30946851501 @default.
- W3094685150 hasRelatedWork W1984164671 @default.
- W3094685150 hasRelatedWork W2319957515 @default.
- W3094685150 hasRelatedWork W2351606222 @default.
- W3094685150 hasRelatedWork W2367613388 @default.
- W3094685150 hasRelatedWork W2369844778 @default.
- W3094685150 hasRelatedWork W2388693422 @default.
- W3094685150 hasRelatedWork W2924180394 @default.
- W3094685150 hasRelatedWork W3014407337 @default.
- W3094685150 hasRelatedWork W3094685150 @default.
- W3094685150 hasRelatedWork W4283079747 @default.
- W3094685150 hasVolume "74" @default.
- W3094685150 isParatext "false" @default.
- W3094685150 isRetracted "false" @default.
- W3094685150 magId "3094685150" @default.
- W3094685150 workType "article" @default.