Functionality of Succinylated Brazil Nut (Bertholletia excelsa HBK) Kernel Globulin

Ramos, Cíntia Maria Pinto; Bora, Pushkar Singh

doi:10.1007/s11130-005-2533-0

Cited by 18 publications

(9 citation statements)

References 24 publications

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“…1). This profile is quite similar with those of soybean meal proteins and other nut proteins from defatted cashew nut, walnut and brazil nut (Neto, Narain, Silva, & Bora, 2001;Ogunwolu, Henshaw, Mock, Santros, & Awonorin, 2009;Ramos & Bora, 2005;Swamylingappa & Srinivas, 1994;Sze-Tao & Sathe, 2000). For HPI-AW, HPC-AW-H and HPI, the maximal solubility was observed at pH 2.0 while HPI-H showed 2.5e3.0 fold lower solubility then these proteins at the indicated acidic pH value.…”

Section: Protein Solubility Of Isolated Hazelnut Meal Proteinssupporting

confidence: 71%

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

et al. 2014

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a b s t r a c tThis study aimed characterization of bioactive, functional and edible film making properties of isolated proteins from untreated (HPI), hot extracted (HPI-H), acetone washed (HPI-AW), and acetone washed and hot extracted (HPC-AW-H) hazelnut meals. The most bioactive protein extract was HPC-AW-H, followed by HPI-AW, HPI-H and HPI, based on antioxidant activity (TEAC and ORAC: 158 e461 mmol Trolox/kg), iron chelation (60.7e126.7 mmol EDTA/kg), angiotensin-converting enzyme inhibition (IC 50 : 0.57e1.0 mg/mL) and antiproliferative activity on colon cancer cells (IC 50 : 3.0e4.6 mg/ ml). Protein contents of HPI, HPI-H and HPI-AW (93.3e94.5%) were higher than that of HPC-AW-H (86.0%), but HPC-AW-H showed the best pH-solubility profile. The extracts showed good oil absorption (7.4e9.4 g/g) and foaming, but limited water holding and gelling capacities, and emulsion stability. The protein extracts gave transparent, yellowish to brownish and reddish colored and water soluble edible films. The HPI gave the lightest colored films with acceptable mechanical properties (elongation up to 144% and tensile strength up to 4.9 MPa). 1-D and 2-D electrophoresis clearly showed the molecular and isoelectric profiles of hazelnut proteins. The overall results of this study showed that the bioactive, solubility and gelation properties of hazelnut proteins could be improved by simple processes like acetone washing and/or heat treatment. The hazelnut proteins are valuable as multipurpose food ingredients.

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Section: Protein Solubility Of Isolated Hazelnut Meal Proteinssupporting

confidence: 71%

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

et al. 2014

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“…Increase in WBC of 11S peptides (6C to 12C) and 7S peptides (16C to 18C) could be attributed by exposure of more charged amino groups as a result of enzymatic hydrolysis and acylation (Figure 4A). The unfolding of protein chains exposes buried amino acid residues making them available for interactions with aqueous medium (Ramos and Bora 2005). Decrease in WBC of acylated UFTW < 3 kDa may be because of high water solubility plus reduction in positively charged group following attachment of acyl residues.…”

Section: Discussionmentioning

confidence: 99%

Improving Surface Functional Properties of Tofu Whey‐Derived Peptides by Chemical Modification with Fatty Acids

Matemu¹,

Katayama²,

Kayahara³

et al. 2012

Journal of Food Science

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Effect of acylation with saturated fatty acids on surface functional properties of tofu whey-derived peptides was investigated. Tofu whey (TW) and soy proteins (7S, 11S, and acid-precipitated soy protein [APP]) were hydrolyzed by Protease M 'Amano' G, and resulting peptide mixtures were acylated with esterified fatty acids of different chain length (6C to 18C) to form a covalent linkage between the carboxyl group of fatty acid and the free amino groups of peptide. Acylation significantly (P < 0.05) increased emulsifying properties of 7S, 11S, and APP peptides independent of fatty acid chain length. Acylation decreased water binding capacity although oil binding capacity of acylated tofu whey ultra filtered fraction (UFTW < 3 kDa), 7S- and 11S-peptides were improved compared to native peptides. 7S peptides acylated with long chain fatty acids had shown significant higher surface hydrophobicity as in contrast with acylated UFTW < 3 kDa and APP peptides. Fluorescence spectra studies revealed structural conformation of acylated soy peptides as compared to native peptides. This study shows that chemical modification with fatty acids can further affect functional properties of soy proteins.

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“…Succinylation also improved the solubility of the Bambara groundnut protein (Table 1) by 3.08% in the succinylated sample compared to its unmodified counterpart [25]. The sample Brazil nut modified with succinylation was nearly 13% greater than its unmodified part [31]. The modification of the cowpea protein sample by succinylation increased its solubility by nearly 47% [28].…”

Section: Solubilitymentioning

confidence: 91%

Impact of Hydrolysis, Acetylation or Succinylation on Functional Properties of Plant-Based Proteins: Patents, Regulations, and Future Trends

Heredia-Leza

Chuck‐Hernández

2022

Processes

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Nowadays, plant-based proteins are gaining momentum due to their wide availability, good amino acid content, and their market appeal. Unfortunately, these molecules usually have low water solubility, affecting other functional characteristics, such as foaming and emulsification, opening technological opportunities for research. Some plant-based protein applications rely on adjustments to final formulations and changing these chemical structures to produce new protein ingredients is also a path widely used in recent research. These modifications can be classified as physical or chemical, the latter being the most popular, and hydrolysis is one of the more widely reported modifications. This review explores the application of chemical modifications to plant-based proteins to improve techno-functional properties, when applied as part of food formulations. In addition, acetylation and succinylation, as the second and third most used processes, are discussed, including a deep analysis of their effects. Furthermore, since there is no concise compilation of patents associated with these technological efforts, some of the references that involve chemical modifications and current regulations used worldwide for novel foods produced with these technologies are included in this review. Finally, future perspectives for the chemical modification of proteins are discussed.

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Functionality of Succinylated Brazil Nut (Bertholletia excelsa HBK) Kernel Globulin

Cited by 18 publications

References 24 publications

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

Bioactive, functional and edible film-forming properties of isolated hazelnut (Corylus avellana L.) meal proteins

Improving Surface Functional Properties of Tofu Whey‐Derived Peptides by Chemical Modification with Fatty Acids

Impact of Hydrolysis, Acetylation or Succinylation on Functional Properties of Plant-Based Proteins: Patents, Regulations, and Future Trends

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