Properties of acetylated potato protein preparations

Miedzianka, Joanna; Pęksa, Anna; Aniołowska, Magda

doi:10.1016/j.foodchem.2011.08.080

Cited by 34 publications

(33 citation statements)

References 45 publications

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“…In terms of ash content, all studied isolates displayed its low amounts (not more than 1.98% found in PIV). According to some authors (van Koningsveld et al 2001;Miedzianka et al 2012) conducting the thermal coagulation of protein contained in potato juice at increased ionic strength by means of salt addition has several advantages. First of all, it ensures a high protein yield and decreases the temperature of coagulation to 65-70°C.…”

Section: Resultsmentioning

confidence: 99%

Amino acid composition of enzymatically hydrolysed potato protein preparations

Pęksa¹,

Miedzianka²

2014

Czech J. Food Sci.

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PĘksa A., Miedzianka J. (2014): Amino acid composition of enzymatically hydrolysed potato protein preparations. Czech J. Food Sci., 32: 265-272.We determine the effects of the technology of obtaining potato protein preparation and of different variants of enzymatic hydrolysis on the chemical and amino acid compositions of the hydrolysates obtained. Potato protein concentrates obtained through their thermal coagulation in potato juice with calcium chloride, calcium lactate or without salt addition were subjected to enzymatic hydrolysis using two commercial hydrolytic enzymes: endopeptidase (Alcalase) and exopeptidase (Flavourzyme). Chemical (contents of ash, total and coagulable protein) and amino acid compositions of the hydrolysates obtained were determined. On the ground of the findings it was stated that the type of potato protein preparation used and conditions of enzymatic modification influenced on the properties of the hydrolysates obtained. Preparations obtained during the study were characterised by similar chemical and amino acid compositions, whereas the preparation obtained through thermal coagulation with the use of calcium lactate contained insignificantly more protein and essential amino acids. The least liable to enzymatic hydrolysis was the preparation obtained by using calcium chloride, particularly when only endopeptidase was used. The application of endopeptidase enzyme enabled to obtain 60% of proteolysis efficiency and the addition of the second enzyme (exopeptidase) to the protein solution insignificantly increased the proteolysis efficiency (to ca 70%), mainly when the preparation coagulated with the use of calcium chloride was hydrolysed. Proteolysis of the protein preparations obtained with the use of two enzymes was more favourable, particularly due to the quantity of free amino acids in and amino acids composition of the hydrolysates.

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Section: Resultsmentioning

confidence: 99%

Amino acid composition of enzymatically hydrolysed potato protein preparations

Pęksa¹,

Miedzianka²

2014

Czech J. Food Sci.

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“…Acylation with acid anhydride has been used to improve the functional properties of various proteins. [6][7][8] The ε-NH 2 at the protein surface easily reacts with acid anhydride such as acetic anhydride, propionic anhydride, maleic anhydride and succinic anhydride. Acylation reduces the positive charges of the ε-NH 2 affected amino acids and dominates the negative charges of the proteins.…”

Section: Introductionmentioning

confidence: 99%

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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“…The most common system of protein recovery from industrial PFJ includes heat coagulation and acid precipitation. Although thermal/ acidic precipitation results in a high yield of protein recovery, it often leads to complete loss of the protein functionality, which limits their application only to animal feed and low-quality fertilizers [16] . Lots of recovery techniques have been explored for the recovery of native protein isolation, including salt precipitation [6] , organic solvent precipitation [6,17] , carboxymethyl cellulose (CMC) complexation [7] , chromatographic techniques [8,9] , ultrafiltration, [10] and the combination of the methods above.…”

Section: Introductionmentioning

confidence: 99%

Comparative study of potato protein concentrates extracted using ammonium sulfate and isoelectric precipitation

Zhang

Sun

et al. 2017

International Journal of Food Properties

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In this study, effects of NaCl concentrations (0.0, 0.2, 0.4, 0.6, 0.8, and 1.0 M) and pH (3.0, 5.0, 7.0, and 8.0) on the physico-chemical and functional properties of potato protein concentrates extracted from potato fruit juice (PFJ) using ammonium sulfate precipitation (ASP) and isoelectric precipitation (IEP) were investigated. The total polyphenol content of potato protein concentrates extracted by IEP (IEPP) was 2.5 times of that of potato protein concentrates extracted by ASP (ASPP), which resulted in the color of IEPP darker than that of ASPP. More protein fractions (74, 62, and 35 kDa) were found in IEPP compared to ASPP. ASPP exhibited higher solubility than IEPP. The emulsifying properties of ASPP and IEPP increased along with the increasing NaCl concentration. ASPP and IEPP showed the lowest emulsifying properties and foaming ability at pH 5.0. While the foaming stability of ASPP and IEPP achieved the maximum and minimum at pH 5.0, respectively. Two endothermic peaks were observed in ASPP at pH 3.0, 8.0, and higher NaCl concentration (≥0.6 M), while more than two endothermic peaks were observed in IEPP at all NaCl concentrations (0.2-1.0 M) and pH values (3.0, 5.0, 7.0, and 8.0). The glutamic acid concentration of ASPP and aspartic acid concentration of IEPP were the highest, while histidine was the lowest according to the amino acid profile of both ASPP and IEPP. In terms of an essential amino acid index with respect to a reference protein of FAO/WHO, the nutritional values of IEPP were higher than those of ASPP.

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Properties of acetylated potato protein preparations

Cited by 34 publications

References 45 publications

Amino acid composition of enzymatically hydrolysed potato protein preparations

Amino acid composition of enzymatically hydrolysed potato protein preparations

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

Comparative study of potato protein concentrates extracted using ammonium sulfate and isoelectric precipitation

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