In vitro digestion of soymilk using a human gastric simulator: Impact of structural changes on kinetics of release of proteins and lipids

Abstract A study was conducted to determine effects of pretreating and supplementing soybean hulls with multi-enzyme on porcine in vitro digestion and fermentation characteristics. Treatments were untreated and heat-pretreated (160 °C and 70 psi for 20 min) soybean hulls without or with multi-enzyme in a 2 × 2 factorial arrangement. The multi-enzyme supplied 2,800 U of cellulase, 1,800 U of pectinase, 400 U of mannanase, 1,000 U of xylanase, 600 U of glucanase, and 200 U of protease/kilogram of feedstuff. Feedstuffs were subjected to in vitro digestion with porcine pepsin and pancreatin, followed by in vitro fermentation for 72 h. Accumulated gas production was recorded and modeled to estimate kinetics of gas production. On DM basis, untreated and pretreated soybean hulls contained 10.4 and 10.6% CP, and 63.2 and 49.5% ADF, respectively. Pretreatment and multi-enzyme supplementation did not interact on in vitro digestibility of DM (IVDDM). Untreated and pretreated soybean hulls did not differ in IVDDM (24.8 vs. 25.7%). Multi-enzyme increased (P < 0.05) IVDDM of soybean hulls by a mean of 45.5%. Pretreatment and multi-enzyme unaffected total gas production. Pretreatment and multi-enzyme interacted (P < 0.05) on fractional rate of degradation such that the fractional rate of degradation for pretreated soybean hulls was greater (P < 0.05) than that of untreated soybean hulls when soybean hulls were supplemented with multi-enzyme (0.045 vs. 0.062 h-1), but not when soybean hulls were unsupplemented with multi-enzyme (0.053 vs. 0.059 h-1). In conclusion, multi-enzyme supplementation increased IVDDM, implying that the multi-enzyme used in the study can be used to enhance utilization of soybean hulls. Heat pretreatment increased the rate of fermentation of multi-enzyme-supplemented soybean hulls, implying that the rate of fermentation of soybean hulls in the hindgut of pigs can be enhanced by a combination of heat pretreatment and multi-enzyme supplementation.

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Effect of emulsifiers on linseed oil emulsion structure, lipolysis and oxidation during in vitro digestion

Food & Function ◽

10.1039/d0fo02072a ◽

2020 ◽

Vol 11 (11) ◽

pp. 10126-10136

Author(s):

Sophie Lamothe ◽

Émilie Jolibois ◽

Michel Britten

Keyword(s):

Lipid Oxidation ◽

Structural Changes ◽

Linseed Oil ◽

In Vitro Digestion ◽

Oil Emulsion

The type of emulsifier determines the structural changes of emulsions, lipolysis and lipid oxidation during in vitro digestion.

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Structural changes of filling creams after in vitro digestion. Application of hydrocolloid based emulsions as fat source

LWT ◽

10.1016/j.lwt.2019.05.121 ◽

2019 ◽

Vol 112 ◽

pp. 108223 ◽

Cited By ~ 2

Author(s):

M. Espert ◽

J. Borreani ◽

I. Hernando ◽

A. Quiles ◽

T. Sanz ◽

...

Keyword(s):

Structural Changes ◽

In Vitro Digestion

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Kinetics of In Vitro Digestion of Starches Monitored by Time-Resolved1H Nuclear Magnetic Resonance

Biomacromolecules ◽

10.1021/bm8014413 ◽

2009 ◽

Vol 10 (3) ◽

pp. 638-644 ◽

Cited By ~ 14

Author(s):

Anthony C. Dona ◽

Guilhem Pages ◽

Robert G. Gilbert ◽

Marianne Gaborieau ◽

Philip W. Kuchel

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

In Vitro Digestion ◽

Kinetics Of ◽

Nuclear Magnetic

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Applicability of an In-Vitro Digestion Model to Assess the Bioaccessibility of Phenolic Compounds from Olive-Related Products

Molecules ◽

10.3390/molecules26216667 ◽

2021 ◽

Vol 26 (21) ◽

pp. 6667

Author(s):

Patricia Reboredo-Rodríguez ◽

Carmen González-Barreiro ◽

Elena Martínez-Carballo ◽

Noelia Cambeiro-Pérez ◽

Raquel Rial-Otero ◽

...

Keyword(s):

Phenolic Compounds ◽

Structural Changes ◽

Virgin Olive Oil ◽

In Vitro Digestion ◽

Current Status ◽

Human Organism ◽

Olive Leaves ◽

Functional Value ◽

Before And After

The Mediterranean diet includes virgin olive oil (VOO) as the main fat and olives as snacks. In addition to providing nutritional and organoleptic properties, VOO and the fruits (olives) contain an extensive number of bioactive compounds, mainly phenolic compounds, which are considered to be powerful antioxidants. Furthermore, olive byproducts, such as olive leaves, olive pomace, and olive mill wastewater, considered also as rich sources of phenolic compounds, are now valorized due to being mainly applied in the pharmaceutical and nutraceutical industries. The digestive system must physically and chemically break down these ingested olive-related products to release their phenolic compounds, which will be further metabolized to be used by the human organism. The first purpose of this review is to provide an overview of the current status of in-vitro static digestion models for olive-related products. In this sense, the in-vitro gastrointestinal digestion methods are widely used with the following aims: (i) to study how phenolic compounds are released from their matrices and to identify structural changes of phenolic compounds after the digestion of olive fruits and oils and (ii) to support the functional value of olive leaves and byproducts generated in the olive industry by assessing their health properties before and after the gastrointestinal process. The second purpose of this review is to survey and discuss all the results available to date.

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Effect of propan-2-ol on enzymic and structural properties of elongation factor G

Biochemical Journal ◽

10.1042/bj2610725 ◽

1989 ◽

Vol 261 (3) ◽

pp. 725-731 ◽

Cited By ~ 5

Author(s):

M Masullo ◽

G Parlato ◽

E De Vendittis ◽

V Bocchini

Keyword(s):

Conformational Changes ◽

Structural Changes ◽

Elongation Factor ◽

Elongation Factor G ◽

Fluorescence Measurements ◽

Different Temperatures ◽

Number Of Binding Sites ◽

Kinetics Of ◽

Factor G

Elongation factor G (EF-G) can support a GTPase activity in vitro even in the absence of ribosomes when propan-2-ol is present [GTPasep; De Vendittis, Masullo & Bocchini (1986) J. Biol. Chem. 261, 4445-4450]. In the present work the GTPasep activity of EF-G was further studied by investigating (i) the effect of ionic environment on GTPasep and (ii) the influence of propan-2-ol on the molecular structure of EF-G as determined by fluorescence and c.d. measurements. In the presence of 1-300 mM univalent cations (M+) alone, no detectable GTPasep activity was measured; however, in the presence of 1 mM-Mg2+ a considerable stimulation was observed at 40 mM-Li+ or 75 mM-NH4+. Among bivalent cations (M2+), 1 mM-Sr2+, 2-5 mM-Ca2+ and 1 mM-Ba2+ were the most effective, but, in the presence of 75 mM-NH4+, Mg2+ and Mn2+ became the most efficient, whereas the stimulation by other M2+ species was considerably decreased. C.d. measurements showed that the alcohol increased the mean molar residue ellipticity of EF-G at 285 nm, but not at 220 nm. As estimated from fluorescence measurements, in the presence of 20% (v/v) propan-2-ol the value of the dissociation constant of the complex formed between EF-G and 8-anilino-1-naphthalene-sulphonate decreased from 8 to 5 microM; similarly, the number of binding sites on EF-G for the fluorescent probe decreased from 13 to 6. Finally, the alcohol enhanced the quenching of the intrinsic fluorescence of EF-G caused by either acrylamide or KI. The data support the hypothesis that propan-2-ol induces moderate conformational changes of EF-G that make the catalytic centre accessible to the substrate even in the absence of ribosomes. Kinetics of GTPasep studied at different temperatures did not reveal additional structural changes of EF-G occurring with time or temperature.

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