Oat protein solubility and emulsion properties improved by enzymatic deamidation

Jiang, Zhongqing; Sontag‐Strohm, Tuula; Salovaara, Hannu; Sibakov, Juhani; Kanerva, Päivi; Loponen, Jussi

doi:10.1016/j.jcs.2015.04.010

Cited by 107 publications

(71 citation statements)

References 27 publications

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“…Second, components, other than β-glucan, present in the oats, such as starch, proteins, galactolipids, and phytochemicals (e.g., phenolic compounds and phytosterols) may have interfered, alone or in combination, with lipolysis. All these oat compounds, together with the β-glucan, may contribute to the hindrance of lipid digestion at different stages of the digestion process, for instance, during emulsification, micelle formation, removal of the lipid products from the interface, and by inhibition of lipase ( Cai et al, 2012 , Chu et al, 2009 , Jiang et al, 2015 ). Fig.…”

Section: Resultsmentioning

confidence: 99%

The impact of oat structure and β-glucan on in vitro lipid digestion

Grundy

Quint

Rieder

et al. 2017

Journal of Functional Foods

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Section: Resultsmentioning

confidence: 99%

The impact of oat structure and β-glucan on in vitro lipid digestion

Grundy

Quint

Rieder

et al. 2017

Journal of Functional Foods

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“…As mentioned above, PG is thought to be one of the most promising protein-deamidation enzymes and has been used to modify many proteins, including wheat gluten ( Yong et al, 2006 ), α-Lactalbumin ( Gu et al, 2001 ), α-zein ( Yong et al, 2004 ), rice glutelin ( Liu et al, 2011 ), skim milk ( Miwa et al, 2010 ), soy protein ( Suppavorasatit et al, 2011 ), yogurt ( Miwa et al, 2014 ), and oat protein ( Jiang et al, 2015 ). Miwa et al (2013) investigated the effect of PG on heat-induced conformational changes in whey protein isolate and its relation to gel properties.…”

Section: Discussionmentioning

confidence: 99%

Complete Genome Sequence and Characterization of a Protein-Glutaminase Producing Strain, Chryseobacterium proteolyticum QSH1265

Zhu

Tian

et al. 2018

Front. Microbiol.

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Recently, an enzyme named protein-glutaminase (PG) has been identified as a new type of enzyme with significant potential for deamidation of food proteins. The enzyme is shown to be expressed as a pre-pro-protein with a putative signal peptide of 21 amino acids, a pro-sequence of 114 amino acids, and a mature PG of 185 amino acids. The microbial enzyme PG specifically catalyzes deamidation of proteins without protein hydrolysis pretreatment and only reacts with glutamine residues in the side-chains of proteins or long peptides. All these attributes suggest that it has a great potential for food industrial applications. However, until recently, there have been relatively few studies of the PG-producing strains. A strain named Chryseobacterium proteolyticum QSH1265 which can produce PG was isolated from a soil sample collected in Songjiang, Shanghai, China. Its enzyme activity was about 0.34 ± 0.01 U/mL when using carboxybenzoxy-Gln-Gly as a substrate. The strain can produce acid from D-glucose, maltose, L-arabinose sucrose, glycerol, and mannitol but not fructose, and it is also positive for indole production and urease. Here we describe the complete genome sequence of this strain via PacBio RSII sequencing. The C. proteolyticum QSH1265 genome consists of a circular chromosome with total length of 4,849,803 bp without any plasmids. All of 4563 genes were predicted including 4459 genes for protein-coding and 104 RNA-relative genes with an average G+C content of 36.16%. The KEGG and COG annotation provide information for the specific function of proteins encoded in the genome, such as proteases, chromoproteins, stress proteins, antiporters, etc. A highly conserved hypothetical protein shares a promoter with the gene encoding the protein-glutaminase enzyme. The genome sequence and preliminary annotation provide valuable genetic information for further study of C. proteolyticum.

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“…Consequently, proteins with high proportion of Gln, as compared with their counterpart proteins with Glu in large proportion, are likely to have lower solubility in aqueous solvents. Deamidation of proteins with high amounts of Gln (e.g., corn, oat, and wheat proteins) assists in improving their solubility (Jiang et al, ; Yong, Yamaguchi, Gu, Mori, & Matsumura, ; Yong, Yamaguchi, & Matsumura, ). Charged side chains on a native protein seem to be most accessible to the solvent and are, therefore, expected to improve protein solubility in aqueous solvent (Malissard & Berger, ; Pace, Trevino, Prabhakaran, & Scholtz, ).…”

Section: Factors That Influence Protein Solubilitymentioning

confidence: 99%

Protein Solubilization

Sathe

Zaffran

Gupta

et al. 2018

J Americ Oil Chem Soc

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To address the anticipated global need for increased protein supply for human nutrition, particularly for developing and underdeveloped regions, concerted efforts are required. Although animal proteins satisfy nutrition needs, they may not be acceptable to all consumers either due to their cost or dietary restrictions followed by the consumer. Soybean has served as a nonanimal protein source; however, alternative protein sources will need to be cultivated and explored in the future to satisfy anticipated increased global needs. To effectively utilize a food protein source, separation of proteins from the nonprotein components present in that source is often needed or desired. Such separation requires understanding of protein properties and interactions of the protein with its environment. In chemical separation processes, protein solubility is a critical property as it often governs protein preparation and utilization and is the focus of this review. Emphasis is on nontraditional protein sources. J Am Oil Chem Soc (2018) 95: 883-901 884 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901 1:100 c 2-98 Thompson, 1977 885 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901 J Am Oil Chem Soc J Am Oil Chem Soc (2018) 95: 883-901

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Oat protein solubility and emulsion properties improved by enzymatic deamidation

Cited by 107 publications

References 27 publications

The impact of oat structure and β-glucan on in vitro lipid digestion

The impact of oat structure and β-glucan on in vitro lipid digestion

Complete Genome Sequence and Characterization of a Protein-Glutaminase Producing Strain, Chryseobacterium proteolyticum QSH1265

Protein Solubilization

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