Protease susceptibility and amino group accessibility to trinitrobenzenesulfonic acid of legumin during its glycosylation

Caer, Daniele.; Colas, Bernard

doi:10.1021/jf00028a007

Cited by 16 publications

(5 citation statements)

References 14 publications

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“…However, the phenol levels are very low in Rhodophycae (Mabeau & Fleurence, 1993). Some studies have shown that high rates of glycosylation could decrease the rate of hydrolysis of enzymes like trypsin and chymotrypsin (Caer & Colas, 1993).…”

Section: Discussionmentioning

confidence: 99%

Evaluation of protein in vitro digestibility of Palmaria palmata and Gracilaria verrucosa

et al. 2005

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Palmaria palmata and Gracilaria verrucosa are edible red seaweeds and potential protein sources for human or animal nutrition, so studies were conducted on their in vitro protein digestibility. After 30 min predigestion by pepsin followed by 6 h digestion into a cell dialysis containing porcine pancreatin, the in vitro protein digestibility of P. palmata and G. verrucosa, expressed in regard to casein digestibility, was 4.9% and 42.1%, respectively. The level of protein digestibility seems to be related to the amount of soluble fibre, which was 45.3% and 30.5%, respectively.

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Section: Discussionmentioning

confidence: 99%

Evaluation of protein in vitro digestibility of Palmaria palmata and Gracilaria verrucosa

et al. 2005

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“…The enhancement of negatively charged groups on the surface of SG would lead to a shift of hydrophobic clusters initially exposed on the surface, toward the interior of the SG molecules, or the masking of the hydrophobic groups from the applied fluorescence probe (ANS̅ ). Caer and Colas 29 observed that the glycation with mono-or disaccharides increased the steric hindrance of legumin, and as a consequence, the protease susceptibility decreased. A similar decrease in H 0 has been observed for SG glycated with glucose 6 or κ-carrageenan.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

Molecular Mechanism for Improving Emulsification Efficiency of Soy Glycinin by Glycation with Soy Soluble Polysaccharide

Peng

Liu

et al. 2018

J. Agric. Food Chem.

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Glycation with carbohydrates has been considered to be an effective strategy to improve the emulsifying properties of plant storage globulins, but the knowledge is inconsistent and even contradictory. This work reported that the glycation with soy soluble polysaccharide (SSPS) progressively improved the emulsification efficiency of soy glycinin (SG) in a degree-of-glycation (DG)-dependent manner. The glycation occurred in both the acidic (A) and basic (B) polypeptides to a similar extent. The physicochemical and structural properties of glycated SG samples with different DG values of 0−35% were characterized. The emulsifying properties of unglycated and glycated SG were performed on the emulsions at an oil fraction of 0.3 and a protein concentration in the aqueous phase, produced using microfluidization as the emusification process. The glycation with increasing the DG led to a progressive decrease in solubility and surface hydrophobicity but remarkably increased the magnitude of ζ-potential. Dynamic latter scattering and spectroscopic results showed that the glycation resulted in a gradual dissociation of the 11S-form SG at the quaternary level (into different [AB] subunits), in a DG-dependent way, while their tertiary ([AB] subunits) and secondary structure were slightly affected. Besides the emulsification efficiency, the glycation progressively accelerated the droplet flocculation and facilitated the adsorption of the proteins at the interface and formation of bridged emulsions. The results demonstrated that the improvement of the emulsification efficiency of SG by the glycation with SSPS was largely attributed to the enhanced conformation flexibility at the [AB] subunit level as well as facilitated formation of bridged emulsions. It was also confirmed that once the glycated SG adsorbed at the interface, it would readily dissociated into subunits; the dissociated [AB] subunits exhibited an outstanding Pickering stabilization. The findings would be of importance for providing new knowledge about the molecular mechanism for the modification of emulsifying properties of oligomeric globulins by the glycation with polysaccharides.

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“…In contrast, in their exhaustive review, Branza-Nichita et al (52) reported that the N-glycosylation of mammalian PPO occurs in the very early stages of PPO synthesis and that the introduced carbohydrate residues contribute to the formation of the enzyme's specific conformation and to copper loading. Also, it has been reported that the nature of glycosylated carbohydrate and the degree of glycosylation may affect the affinity of proteases to their substrates (53,54). Thus, in addition to different protease profiles, PPO availability may also be effective on the formation and destabilization of TS-PPO enzyme in apricots.…”

Section: Characterization Of Ts-ppomentioning

confidence: 99%

Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

Yemenicioğlu

Cemeroğlu

2003

J. Agric. Food Chem.

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Destabilization of thermostable polyphenol oxidase (TS-PPO) during the ripening of peaches has been previously shown (Yemenicioǧ lu, A.; Cemeroǧ lu, B. Tr. J. Agric. For. 1998, 22, 261-265). This work studied the effect of ripening on thermal stability of apricot PPO for three different cultivars. Kabaaş ı cultivar contained thermolabile PPO, whereas TS-PPO appeared in Hacıhaliloǧ lu and Ç ataloǧ lu cultivars. The TS-PPO showed biphasic inactivation curves, and its D and z values between 60 and 90°C varied in the ranges of 357-1.12 min and 11.9-12.7°C, respectively. In Hacıhaliloǧ lu cultivar the TS-PPO was very consistent and existed at all stages of ripening, whereas in Ç ataloǧ lu cultivar it appeared only at the half-ripe stage. The loss of consistent TS-PPO in Hacıhaliloǧ lu apricots after partial purification by acetone precipitation and DEAE-cellulose chromatography suggested the non-covalent nature of its stabilization. The main purified fractions (F1 and F2) showed monophasic inactivation curves with similar thermal inactivation parameters (z F1 ) 10.4°C, z F2 ) 10.1°C). However, their kinetic properties against catechol (K mF1 ) 61 mM, K mF2 ) 122.7 mM) and substrate specificities were considerably different. The results of this study showed the presence of TS-PPO forming and destabilizing mechanisms in apricots. Further studies are needed for the solution of these mechanisms and to develop some new strategies that may be utilized by molecular techniques for a planned production of apricot cultivars provided with heat labile but normal PPO activity.

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Protease susceptibility and amino group accessibility to trinitrobenzenesulfonic acid of legumin during its glycosylation

Cited by 16 publications

References 14 publications

Evaluation of protein in vitro digestibility of Palmaria palmata and Gracilaria verrucosa

Evaluation of protein in vitro digestibility of Palmaria palmata and Gracilaria verrucosa

Molecular Mechanism for Improving Emulsification Efficiency of Soy Glycinin by Glycation with Soy Soluble Polysaccharide

Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

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