Influence of succinylation on physicochemical property of yak casein micelles

Min, Yang; Yang, Jianjun; Yuan, Zhe; Zhang, Weibing

doi:10.1016/j.foodchem.2015.06.030

Cited by 21 publications

(10 citation statements)

References 33 publications

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“…The decreased S 0 in the succinylated proteins could be due to the presence of a higher net negative charge at the surface of protein molecules, affecting the ability of the ANS − probe to bind to the polar sites because of high electrostatic repulsion. Similar trends were found in soy protein hydrolysate, [28] kidney bean protein isolate, [8] sodium caseinate, [13] milk protein concentrate, [12] yak casein micelles [29] and whey protein concentrate. [30] Other studies suggested that the decreasing of S 0 of succinylated proteins could be attributed to the polarity of the succinylated proteins where a higher amount of polar charged groups or a relatively lower amount of non-polar groups at the protein surface resulting in the increasing of the net charge.…”

Section: Influence Of Succinylation On the Surface Hydrophobicity Of supporting

confidence: 75%

“…[30] Other studies suggested that the decreasing of S 0 of succinylated proteins could be attributed to the polarity of the succinylated proteins where a higher amount of polar charged groups or a relatively lower amount of non-polar groups at the protein surface resulting in the increasing of the net charge. [12,28,29] In addition, stearic hindrance could also cause the reduction of the S 0 of succinylated proteins, attributed to the structural modification of proteins upon succinylation. [12,29] Influence of succinylation on the protein solubility…”

Section: Influence Of Succinylation On the Surface Hydrophobicity Of mentioning

confidence: 99%

“…[12,28,29] In addition, stearic hindrance could also cause the reduction of the S 0 of succinylated proteins, attributed to the structural modification of proteins upon succinylation. [12,29] Influence of succinylation on the protein solubility…”

Section: Influence Of Succinylation On the Surface Hydrophobicity Of mentioning

confidence: 99%

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Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation

Charoensuk

Brannan

Chanasattru

et al. 2018

International Journal of Food Properties

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The application of mung bean protein in foods is limited due to its poor functionality. Acylation with succinic anhydride could be used to improve the functionalities of protein. In this study, the influence of the weight ratio of succinic anhydride to protein (0-0.10) on the degree of N-acylation, physicochemical properties and protein functionalities including emulsifying properties of mung bean protein isolates (MPI) were investigated. The extent of N-acylation of MPI increased as the succinic anhydride:protein ratio increased, while the ζ-potential at neutral pH decreased. In addition, succinylation had an impact on the average particle size of MPI depending on the succinic anhydride:protein ratio. Succinylation had no impact on the total and exposed free sulfhydryl groups. Moreover, the isoelectric point (pI) of the succinylated proteins shifted from pH 5 to lower pH. Succinylation increased the emulsifying activity index (EAI), while the impact on the emulsion stability index depended on the succinic anhydride:protein ratio. Thus, succinylation at low succinic anhydride:protein ratio can alter mung bean protein charge and affect physicochemical and functional properties especially emulsifying properties that could be used to increase its utilization.

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Section: Influence Of Succinylation On the Surface Hydrophobicity Of supporting

confidence: 75%

Section: Influence Of Succinylation On the Surface Hydrophobicity Of mentioning

confidence: 99%

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Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation

Charoensuk

Brannan

Chanasattru

et al. 2018

International Journal of Food Properties

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“…The PTM of a protein can also determine the cell signaling state, turnover, localization, and interactions with other proteins [2]. Therefore, the analysis of proteins and their PTMs are particularly important for the study of heart disease, cancer, neurodegenerative diseases and diabetes [3,4]. Although the characterization of PTMs gets invaluable insight into the cellular functions in etiological processes, there are still challenges.…”

Section: Introductionmentioning

confidence: 99%

Opinion Prediction of protein Post-Translational Modification sites: An overview

Hasan¹,

Khatun²

2017

Ann Proteom Bioinform

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BackgroundPost-translational modi ication (PTM) refers to the covalent and enzymatic modi ication of proteins during or after protein biosynthesis. In the protein biosynthesis process, the ribosomal mRNA is translated into polypeptide chains, which may further undergo PTM to form the product of mature protein [1]. PTM is a common biological mechanism of both eukaryotic and prokaryotic organisms, which regulates the protein functions, the proteolytic cleavage of regulatory subunits or the degradation of entire proteins and affects all aspects of cellular life. The PTM of a protein can also determine the cell signaling state, turnover, localization, and interactions with other proteins [2]. Therefore, the analysis of proteins and their PTMs are particularly important for the study of heart disease, cancer, neurodegenerative diseases and diabetes [3,4]. Although the characterization of PTMs gets invaluable insight into the cellular functions in etiological processes, there are still challenges. Technically, the major challenges in studying PTMs are the development of speci ic detection and puri ication methods.The PTMs of proteins have been detected by a variety of experimental techniques including the mass spectrometry (MS) [5,6], liquid chromatography [7], radioactive chemical method [8], chromatin immune precipitation (ChIP) [9], western blotting [10], and eastern blotting [7]. The MS technique is one of the mainstay routes in detecting PTMs in a high-throughput manner. The new MS and capillary liquid chromatography instrumentation have made revolutionary advance in enrichment strategies in our growing knowledge of various PTMs [11]. The last decade of the actual description of many PTMs complexity has emerged through the diverse technologies and thousands of precise modi ication sites can now be identi ied with high con idence [12][13][14][15][16][17][18][19][20]. A similar strategy of fragmentation for PTM identi ication is the beam-type collisioninduced dissociation, also called higher energy collisional dissociation [21]. These types of fragmentation are characterized by the higher activation energy. Most of the fragmentation methods of precursor ions are based on the radical anions or thermal electrons [22]. These methods are advantageous over collisionally activated dissociation methods for detecting the unstable PTMs (e.g. O-GlcNAc and phosphorylation), due to the peptide support fragmentation method is effectively independent of the amino acid sequence [23][24][25]. To date, more than 350 types of PTMs have been experimentally discovered in vivo [26]. The common PTMs are phosphorylation, ubiquitination, succinylation, acetylation, pupylation, sumoylation, glycosylation, and so on. In addition, pupylation referring to the modi ication of lysine residues with a prokaryotic, ubiquitin-like protein (i.e. Pup) is another PTM in bacteria.In general, the experimental analysis of PTMs often requires labor-intensive sample preparations and hazardous or expensive chemical reagents. For instance, in the radioactive...

show abstract

“…The PTM of a protein can also determine the cell signaling state, turnover, localization, and interactions with other proteins [3]. Therefore, the analysis of proteins and their PTMs are particularly important for the study of heart disease, cancer, neurodegenerative diseases and diabetes [4,5]. Since the characterization of PTMs gets invaluable insight into the cellular functions in etiological processes, there are still challenges.…”

mentioning

confidence: 99%