Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds

Bojórquez‐Velázquez, Esaú; Lino-López, Gisela Jareth; Huerta‐Ocampo, José Ángel; Barrera-Pacheco, Alberto; Rosa, Ana; Moreno, Abel; Mancilla-Margalli, N. Alejandra; Osuna-Castro, Juan Alberto

doi:10.1016/j.foodchem.2015.06.099

Cited by 17 publications

(9 citation statements)

References 39 publications

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“…The presence of 2‐mercaptoethanol (reducing conditions) allowed the identification of the mainly four bands with a molecular weight of ~32 kDa and four bands of ~20 kDa, corresponding to the acidic and basic polypeptides, respectively, in addition to minor proteins. This electrophoretic profile was similar to previous reports on isolated chan globulins (Aguirre et al., 2012; Bojórquez‐Velázquez et al., 2016). Besides, ImageLab analyses indicated that the protein content of the CG fraction was around 96%, which is coincident with cashew nut globulin (yield = 95.5% of protein content) and buckwheat globulin (96.7%).…”

Section: Resultssupporting

confidence: 91%

“…Globulins, salt‐soluble storage proteins, represent the major Osborne fraction of leguminous seeds, some cereals such as oats ( Avena sativa ) and rice ( Oryza sativa ) and pseudocereals, including amaranth ( Amaranthus hypochondriacus ), quinoa ( Chenopodium quinoa ), chia ( Salvia hispanica ), and chan ( Hyptis suaveolens L. Poit) seeds (Bojórquez‐Velázquez et al., 2016; Carrazco‐Peña et al., 2013; Mäkinen et al., 2016). Based on their sedimentation coefficients, globulins are classified into two groups: 7S or vicilins and 11S or legumins.…”

Section: Introductionmentioning

confidence: 99%

“…The 11S globulin of chan is composed of four different monomers of around 50 kDa. Under reducing conditions, these are separated into basic and acidic polypeptides of about 32 and 20 kDa, respectively, being the result of cleavage of conserved intermolecular disulfide bonds (Aguirre et al., 2012; Bojórquez‐Velázquez et al., 2016).…”

Section: Introductionmentioning

confidence: 99%

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Thermal and emulsifying properties of globulins from chan ( Hyptis suaveolens L. Poit) seeds

Cruz-Torres

Mancilla-Margalli

VillaVelázquez-Mendoza

et al. 2020

J Food Process Preserv

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This research aims to study the thermal and emulsifying properties of the chan globulins (CG), which are the most abundant Osborne fraction of the seed of Hyptis suaveolens. In this sense, the calorimetric analysis indicated a cooperative behavior in thermal denaturation process with a denaturation temperature of 100.9°C and an enthalpy change of 124.6 kJ/mol for CG. Besides, strong gels (Gʹ ~7.5 × 105 Pa) were produced, with a gelation temperature of 80°C. Also, CG presented high surface activity with critical micelle concentration (CMC) of 0.3 mg/ml. The best emulsifying properties and colloidal stability were found at basic pH values and they were negatively influenced by the content of NaCl along a pH gradient. In conclusion, CG may be used as thermostable emulsifier at basic pH values (preferably without NaCl), and as a potential ingredient for protein‐rich gel formulations. Practical applications This work describes a simple and practical procedure to obtain CG at high yield (96%) and acceptable purity, which could be easily implemented without further costs and tedious chromatographic techniques. In addition, the high gelation capacity and strong gel formation for CG, make them suitable for formulation of protein‐based gels with potential application in the drug and food industry. CG also showed high emulsifying activity and emulsifying stability indexes, implying their promising use as a thermostable emulsifier at basic pH values. Finally, the incorporation of CG as food ingredient, is an alternative to other pseudocereals to expand the offer of gluten‐free food products for celiac consumers.

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Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

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Thermal and emulsifying properties of globulins from chan ( Hyptis suaveolens L. Poit) seeds

Cruz-Torres

Mancilla-Margalli

VillaVelázquez-Mendoza

et al. 2020

J Food Process Preserv

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“…11S globulin (cucurbitin) forms crystalloids in the protein bodies, while 7S globulin and 2S albumin are located in the matrix of the protein bodies (Hegedus et al, 2015). Amandin is an 11S globulin legumin-like protein that is hexameric in form and composed of individual polypeptides (Bojórquez-Velázquez et al, 2016). Each monomeric subunit, like those of other 11S globulins, is comprised of a large 40-42 kDa acidic chain and a small 20-22 kDa basic chain that are linked by a disulfide bond (Natarajan et al, 2013).Two isoforms have been identified in almond, prunin 1 and prunin 2, which comprise native prunin (de la Cruz et al, 2017).…”

Section: Sds-page Analysis Of 11s Globulin Protein Of Sesame Seeds Amentioning

confidence: 99%

Antihypertensive Effect of Peptides from Sesame, Almond, and Pumpkin Seeds: In-silico and In-vivo Evaluation

2018

Agriculture and Life Sciences

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“…30 The signals at 175 and 298 kDa can be assigned to 11S globulin. Bojórquez-Velázquez et al 31 identified 11S globulin in chia seeds with a molecular mass of 150 to 300 kDa, which has four monomeric units of 53.5, 52, 51.1 and 49.5 kDa, each unit consisting of a basic and an acid subunit bound by a disulfide bond. Figure 2b presents the results obtained for extracts of cowpea seeds from extractions assisted by ultrasonic radiation at 50 °C for 20 min using as extractor: water (P10) or buffer (P16).…”

Section: Evaluation Of Biomolecules By Hplc-uvmentioning

confidence: 99%

Sample Preparation Applied to Analysis of Proteins in Cowpea Seeds (Vigna unguiculata (L.) Walp.)

Nascimento

Coelho

Júnior

et al. 2018

J. Braz. Chem. Soc.

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In this study, 20 different protocols for protein extraction of cowpea seeds in natura were evaluated taking into account four parameters: cell disruption method, time, temperature and solvent. Factorial design experiments were executed to determine the effects on the total protein content of extracts. The total protein content was determined and the results were in the range of 8.75 ± 1.3 and 86.6 ± 6.9 mg g-1. The richest protein extracts were obtained using Tris-HCl buffer at 50 °C for 20 min for each assessed cell disruption method. However, the results using water were similar to buffer according to t-test at the 95% confidence level. Six protocols demonstrated higher extraction efficiency. Comparative proteomic study using size exclusion chromatography coupled to diode array detector (SEC-DAD) revealed that the one protocol extracted simultaneously high and low molecular mass biomolecules. In fact, the effect of microwave radiation promoted an increased solubility of biomolecules in water. The analysis of chromatographic profiles for principal component analysis (PCA) highlights the greater efficiency of extraction with the application of this protocol. Therefore, our study showed that the optimum condition for extraction of cowpea seed protein consists of water assisted by microwave radiation at 50 °C for 20 min.

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Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds

Cited by 17 publications

References 39 publications

Thermal and emulsifying properties of globulins from chan ( Hyptis suaveolens L. Poit) seeds

Thermal and emulsifying properties of globulins from chan ( Hyptis suaveolens L. Poit) seeds

Antihypertensive Effect of Peptides from Sesame, Almond, and Pumpkin Seeds: In-silico and In-vivo Evaluation

Sample Preparation Applied to Analysis of Proteins in Cowpea Seeds (Vigna unguiculata (L.) Walp.)

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