Characterization of the protein and peptide of excipient zein by the multi-enzyme digestion coupled with nano-LC-MS/MS

Li, Menglin; Zheng, Hao; Ma, Lin; Zhu, Wenwen; Zhang, Jinlan

doi:10.1016/j.foodchem.2020.126712

Cited by 22 publications

(17 citation statements)

References 38 publications

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“…This basic solution is characterized by containing urea or high concentrations of surfactants. The hydrophobic characteristic is derived from the high content of leucine and alanine [13,[18][19][20]. Other important characteristics of the zein are low water vapor permeability and a greaseproof property [21].…”

Section: Physico-chemical Propertiesmentioning

confidence: 99%

“…Zein is classified into four types, such as α-zein, β-zein, γ-zein and δ-zein. The α-zein represents almost 80% of the total amount of zein, while β and γ-zein are usually present in the range of 10-15% and the rest is δ-zein [18]. The molecular weight of α-zein is about 22 up to 24 kDa, β-zein is around 17 kDa, δ-zein is 10 kDa and γ-zein ranges from 18 to 27 kDa [24].…”

Section: Physico-chemical Propertiesmentioning

confidence: 99%

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A Review of Zein as a Potential Biopolymer for Tissue Engineering and Nanotechnological Applications

Pérez-Guzmán

Castro-Muñoz

2020

Processes

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Tissue engineering (TE) is one of the most challenging fields of research since it provides current alternative protocols and materials for the regeneration of damaged tissue. The success of TE has been mainly related to the right selection of nano-sized biocompatible materials for the development of matrixes, which can display excellent anatomical structure, functionality, mechanical properties, and histocompatibility. Today, the research community has paid particular attention to zein as a potential biomaterial for TE applications and nanotechnological approaches. Considering the properties of zein and the advances in the field, there is a need to reviewing the current state of the art of using this natural origin material for TE and nanotechnological applications. Therefore, the goal of this review paper is to elucidate the latest (over the last five years) applications and development works in the field, including TE, encapsulations of drugs, food, pesticides and bandaging for external wounds. In particular, attention has been focused on studies proving new breakthroughs and findings. Also, a complete background of zein’s properties and features are addressed.

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Section: Physico-chemical Propertiesmentioning

confidence: 99%

Section: Physico-chemical Propertiesmentioning

confidence: 99%

A Review of Zein as a Potential Biopolymer for Tissue Engineering and Nanotechnological Applications

Pérez-Guzmán

Castro-Muñoz

2020

Processes

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“…This is a tremendous increase in depth of analysis compared to previous reports of LC-MS/MS analysis on hydrolysates, where the number of identified peptides is often reported in the tens to low thousands range (Caron et al, 2016;Cui, Sun, Cheng, & Guo, 2022;Hinnenkamp & Ismail, 2021;Y. P. Huang, Dias, Leite Nobrega de Moura Bell, & Barile, 2022;Jin, Yan, Yu, & Qi, 2015;M. Li, Zheng, Lin, Zhu, & Zhang, 2020).…”

Section: 4peptide Identification and Mean Peptide Propertiesmentioning

confidence: 97%

Targeted hydrolysis of native potato protein: A novel route for obtaining hydrolysates with improved interfacial properties

Gregersen

Jafarpour

Yeşiltaş

et al. 2022

Preprint

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Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel approach for producing a potato protein hydrolysate with improved emulsifying and foaming properties by data-driven, targeted hydrolysis. Based on previous studies, we selected 15 emulsifier peptides derived from abundant potato proteins, which were clustered based on sequence identity. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavorzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the target peptides. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp produced a hydrolysate (DH=5.4%) with the highest (P<0.05) emulsifying and foaming abilities, good stabilities, and high aqueous solubility. Using LC-MS/MS, we identified >10,000 peptides in each hydrolysate. Through peptide mapping, we show that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. While Neut hydrolysates had the highest proportion of peptides with target overlap, they showed inferior interfacial activity. In contrast, Tryp was able to release specifically targeted peptides, explaining the high surface activity observed. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that data-driven, targeted hydrolysis is a viable, interdisciplinary approach to facilitate hydrolysis design for production of functional hydrolysates from alternative protein sources.

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“…Other methods of zein separation include chromatographic methods such as reversed-phase HPLC method on C18 column with a gradient of 45 to 75% acetonitrile-ultrapure water, both containing 0.01% trifluoroacetic acid [33] or with acetonitrile-trifuoroacetic acid gradient [34]. Liquid chromatography-mass spectrometry (LC-MS), a method widely used in proteome analysis due to its high sensitivity, was for the first time adopted for zein evaluation in 2020; the authors coupled multi-enzyme digestion with nano-LC-MS/ MS [35]. Separation techniques mentioned here are used for the analysis of protein compositions in biological samples of high complexity [22].…”

Section: Analysis Of Zein Proteinsmentioning

confidence: 99%

Nitrogen Storage in Crops: Case Study of Zeins in Maize

Duvnjak¹,

Kljak²,

Grbeša³

2021

Nitrogen in Agriculture - Physiological, Agricultural and Ecological Aspects [Working Title]

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Crop grains accumulate significant amounts of nitrogen in the form of storage proteins. Grain storage proteins are not only important in the aspects of germination but also, storage proteins are a valuable food source in human and animal nutrition. This chapter will give insight into genotype and growing conditions influencing the quantity and quality of storage proteins, primarily maize storage proteins the leading cereal by world production. Main storage proteins in cereals are prolamins, and in maize prolamins are called zeins located within the endosperm in protein agglomerations called protein bodies. Four main classes of zein proteins are: alpha, beta, gamma and delta zein. Each of four zein classes has a distinctive position and role within protein bodies. Prolamin proteins define nutritional value of maize grain not only via amino acid quality but also via starch availability. Starch, the most important energy component of maize grain, is located within starch-protein matrix. Within this matrix, starch granules are surrounded by protein bodies that limit starch availability. In this chapter, we will describe how zein proteins influence characteristics of maize grain and nutritional value of maize.

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Characterization of the protein and peptide of excipient zein by the multi-enzyme digestion coupled with nano-LC-MS/MS

Cited by 22 publications

References 38 publications

A Review of Zein as a Potential Biopolymer for Tissue Engineering and Nanotechnological Applications

A Review of Zein as a Potential Biopolymer for Tissue Engineering and Nanotechnological Applications

Targeted hydrolysis of native potato protein: A novel route for obtaining hydrolysates with improved interfacial properties

Nitrogen Storage in Crops: Case Study of Zeins in Maize

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