Binding studies of crocin to β-Lactoglobulin and its impacts on both components

Allahdad, Zahra; Khammari, Anahita; Karami, Leila; Ghasemi, Ali; Sirotkin, Vladimir A.; Haertlé, Thomas; Saboury, Ali Akbar

doi:10.1016/j.foodhyd.2020.106003

Cited by 29 publications

(7 citation statements)

References 52 publications

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“…Typically, the hydrophobic groups were hidden in the compact molecule and unfolded as the SASA value increased. In the process of simulating the heating treatment of myosin, both the hydrophobic and hydrophilic SASA curves fluctuated significantly ( Figures 5E, F ), indicating that the conformations of proteins changed during the simulation ( 40 ). The SASA curves of four systems ( Figure 5G ) showed that the secondary structure was significantly changed after heat treatment, which is compatible with the Raman spectroscopy results.…”

Section: Resultsmentioning

confidence: 99%

The degree of doneness affected molecular changes and protein digestibility of pork

Han

Liu²,

Li³

et al. 2023

Front. Nutr.

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The degree of doneness has been shown to have a great impact on eating quality of meat, however, it is little known whether it affects protein digestibility of meat. In this study, we explored molecular changes and protein digestibility of pork under different degree of doneness. Pork chops were cooked in a 100°C water bath for about 26 min and a gradient decrease in doneness was obtained from outer to inner layers of samples. Compared with the raw samples, the cooked samples’ active and total sulfhydryl contents, surface hydrophobicity, and turbidity increased but its solubility decreased. The inner layers with lower doneness contained higher α-helix, and fluorescence intensities of tryptophan and tyrosine residues than the outer layers with higher doneness. The pepsin and pancreatin digestibility of meat proteins in the inner layers were higher than those of the outer layers. Molecular simulation analysis showed that the most abundant protein in pork, i.e., myosin in the outer layers were more stable with an increased number of hydrogen bonds, making it difficult to be digested. These findings provided a new insight into the heterogeneity of meat nutritional quality due to the existence of doneness gradient.

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Section: Resultsmentioning

confidence: 99%

The degree of doneness affected molecular changes and protein digestibility of pork

Han

Liu²,

Li³

et al. 2023

Front. Nutr.

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“…Several factors like easily water-soluble, undesirable fibers, and the small size of powder saffron do not affect the properties of the desired product. The saffron extract is considered more valuable due to its uniform color intensity and no need for preheating treatments ( 9 ).…”

Section: Food Applications Of Crocinmentioning

confidence: 99%

“…Crocin has the highest recorded absorbance at 440 nm ( 8 ). Because of its limited stability, crocins lose its functionality when exposed to light, heat, and acidic nature ( 9 ). Also have low immersion and bioavailability, as it is un-absorbed if taken orally till hydrolyzed to produce deglycosylated trans-crocetin in the intestinal tract by enzymatic conditioning in the intestinal epithelial cells and by the fecal bacteria ( 9 ).…”

Section: Introductionmentioning

confidence: 99%

Crocin: Functional characteristics, extraction, food applications and efficacy against brain related disorders

Ali

Kousar

et al. 2022

Front. Nutr.

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Crocin is a bioactive compound that naturally occurs in some medicinal plants, especially saffron and gardenia fruit. Different conventional and novel methods are used for its extraction. Due to some control conditions, recent methods such as ultrasonic extraction, supercritical fluid extraction, enzyme-associated extraction, microwave extraction, and pulsed electric field extraction are widely used because these methods give more yield and efficiency. Crocin is incorporated into different food products to make functional foods. However, it can also aid in the stability of food products. Due to its ability to protect against brain diseases, the demand for crocin has been rising in the pharmaceutical industry. It also contain antioxidant, anti-inflammatory, anticancer and antidepressant qualities. This review aims to describe crocin and its role in developing functional food, extraction, and bioavailability in various brain-related diseases. The results of the literature strongly support the importance of crocin against various diseases and its use in making different functional foods.

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“…BLG can also interact with various drugs and therefore has been proposed as a potential carrier for many therapeutic agents (Gholami et al, 2021;Ghalandari et al, 2015;Balasco et al, 2020;Kayani et al, 2018). Like most lipocalins, the -lactoglobulin molecule folds as an eight-stranded -barrel, which is the primary ligand-binding site (Allahdad et al, 2020;Dan et al, 2019;Loch et al, 2011Loch et al, , 2012Loch et al, , 2013Loch et al, , 2015Loch et al, , 2018Sawyer, 2013;Patel et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

New ligand-binding sites identified in the crystal structures of β-lactoglobulin complexes with desipramine

Loch¹,

Barciszewski²,

Sliwiak³

et al. 2022

Int Union Crystallogr J

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The homodimeric β-lactoglobulin belongs to the lipocalin family of proteins that transport a wide range of hydrophobic molecules and can be modified by mutagenesis to develop specificity for novel groups of ligands. In this work, new lactoglobulin variants, FAF (I56F/L39A/M107F) and FAW (I56F/L39A/M107W), were produced and their interactions with the tricyclic drug desipramine (DSM) were studied using X-ray crystallography, calorimetry (ITC) and circular dichroism (CD). The ITC and CD data showed micromolar affinity of the mutants for DSM and interactions according to the classical one-site binding model. However, the crystal structures unambiguously showed that the FAF and FAW dimers are capable of binding DSM not only inside the β-barrel as expected, but also at the dimer interface and at the entrance to the binding pocket. The presented high-resolution crystal structures therefore provide important evidence of the existence of alternative ligand-binding sites in the β-lactoglobulin molecule. Analysis of the crystal structures highlighted the importance of shape complementarity for ligand recognition and selectivity. The binding sites identified in the crystal structures of the FAF–DSM and FAW–DSM complexes together with data from the existing literature are used to establish a systematic classification of the ligand-binding sites in the β-lactoglobulin molecule.

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Binding studies of crocin to β-Lactoglobulin and its impacts on both components

Cited by 29 publications

References 52 publications

The degree of doneness affected molecular changes and protein digestibility of pork

The degree of doneness affected molecular changes and protein digestibility of pork

Crocin: Functional characteristics, extraction, food applications and efficacy against brain related disorders

New ligand-binding sites identified in the crystal structures of β-lactoglobulin complexes with desipramine

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