Papers by Munkh-Erdene Baatar
Food Research International, 2009
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Journal of Food Science, 1981
Succinylated cottonseed protein isolates (40% and 54% modification of amino groups of control iso... more Succinylated cottonseed protein isolates (40% and 54% modification of amino groups of control isolate) were prepared under pilot scale processing conditions. Partial succinylation of cottonseed flour increased the yield of protein isolate in isoelectric precipitation (pH 4.5). The succinylated isolates were more water soluble, less heat-coagulable in water, and lighter in color as compared to conventional isolates. They also showed improved functional properties including higher oil absorption, emulsion capacity, gel strength, water hydration, water retention, and viscosity. Bulk density was decreased and resulted in fluffy isolates.
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Food Chemistry, 2002
Two types of protein isolates were prepared from Lupinus angustifolius defatted flour by alkaline... more Two types of protein isolates were prepared from Lupinus angustifolius defatted flour by alkaline extraction, with (Isolate B) and without (Isolate A) sodium sulphite, and acid precipitation of proteins at the isoelectric point (IEP 4.3). Chemical composition, main functional properties and protein composition of L. angustifolius defatted flour and protein isolates were determined. Isolate A and B have 93.9 and 84.6% protein content, respectively, and had a balanced composition of essential amino acids, with respect to the FAO pattern except for lysine. The in vitro protein digestibility ranged between 86.3 and 93.9% for isolate A and B, respectively.
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Journal of Food Engineering, 2007
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Food Chemistry, 1999
Two types of protein isolates were prepared from ground chickpea seeds by alkaline extraction, wi... more Two types of protein isolates were prepared from ground chickpea seeds by alkaline extraction, with (Isolate-B) and without (Isolate-A) sodium sulphite, and acid precipitation of the proteins at the isoelectric point (pI 4.3). The percentage of protein recovered from chickpea flour in the preparation of Isolates-A and B were 65.9 and 62.1%, respectively. Chemical composition, main functional properties and protein composition of chickpea flour and protein isolates were determined. Isolates-A and B contained 78 and 88.1% of protein, respectively, and had a balanced content of essential amino acids, with respect to the FAO pattern. The in vitro protein digestibility ranged between 95.6 and 96.1%. Isolate-A showed a partial dissociation of the 11S protein because of the high pH used for the protein extraction, and this probably explains the differences observed in the functional characteristics of both isolates.
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Journal of Food Science, 1977
ABSTRACT An alkaline extraction process was developed to produce protein isolates and starch from... more ABSTRACT An alkaline extraction process was developed to produce protein isolates and starch from defatted flour or defatted groats of high-protein oats. Optimum extraction was at pH 9.2 in 0.02 N sodium hydroxide with a solid: solvent ratio of 1: 6. The defatted flour was ...
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Plant Foods for Human Nutrition, 2005
Protein isolates from L. campestris and soybean seeds were prepared using isoelectric precipitati... more Protein isolates from L. campestris and soybean seeds were prepared using isoelectric precipitation (PI) and micellization (MI) procedures. The amount of protein recovered was considerably higher with the isoelectric precipitation than with the micellization procedure (60% and 30%, respectively). Protein contents were higher than 90% in protein isolates. Antinutritional factors content (alkaloids, lectins, and tannins) were reduced to innocuous levels after protein isolate preparation. Minimum protein solubility for the precipitated lupin protein isolate (LPI) was at pH 4.0, and between pH 4 and 6 for the micellized lupin protein isolate (LMI), increasing at both extremes of the pH scale. Water absorption for the LMI was 1.3 ml/g of protein and its oil absorption 2.2 ml/g of protein. The LPI had 1.7 ml/g of protein in both water and oil absorption. Foaming capacity and stability was pH-dependent. Foaming capacity was higher at pH 2 and lower near the protein isoelectric points. Minimum protein concentration for gelation in LMI was 8% w/v at pH 4, while for LPI was 6% at pH 4 and 6. Amino acid composition in L. campestris flour and protein isolates was high in lysine and low in methionine. Most of the essential amino acids in lupin protein isolates were at acceptable levels compared to a reference pattern for infants and adults. The electrophoretic pattern of both protein isolates showed three bands with different mobilities, suggesting that the protein fractions belong to α-conglutin (11S-like protein), β-conglutin (7S-like protein) and γ-conglutin. It is proven that some of the functional properties of L. campestris protein isolates are similar to those soybean protein isolates recovered under equal conditions.
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Journal of Food Science, 1984
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Food Chemistry, 2011
In this study, the functional properties of Ginkgo seed protein isolate (GPI), Ginkgo seed globul... more In this study, the functional properties of Ginkgo seed protein isolate (GPI), Ginkgo seed globulin protein (GGP) and Ginkgo seed albumin protein (GAP) extracted from Ginkgo biloba seeds were investigated. The protein contents of GPI, GGP and GAP were 91.0%, 93.4% and 87.8%, respectively in the samples in which the sugar, polyphenol and crude fibre were removed by the preparation procedure. For functional properties of Ginkgo seed proteins in the natural state, GAP showed the highest oil-absorption capacity (9.3 ml/g), foaming capacity (67.8%), emulsifying capacity (65.4%) and emulsion stability (90.6%); while GPI showed the highest water absorption capacity (1.93 ml/g), and GGP showed the highest foam stability (55.5%). The differences of the chemical components, surface hydrophobicity, disulphide bond (SS) and sulfhydryl group (SH) contents of GPI, GGP and GAP, which were correlated significantly with functional properties of Ginkgo seed proteins, were also investigated. The improved functional properties, such as water absorption capacity, solubility, foaming properties and emulsifying properties of Ginkgo seed proteins were observed in a pH range of 8.0–10.0 or sodium chloride concentration of 0.5–0.75 M.
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Journal of Food Science, 1987
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International Journal of Food Properties, 2011
Glutaminase (EC 3.2.1.5) was applied in the present work to deamidate soybean protein isolates wi... more Glutaminase (EC 3.2.1.5) was applied in the present work to deamidate soybean protein isolates with limited extent, and some reaction conditions were selected. Three deamidated soybean protein isolates products with degree of deamidation of 3.5, 5.6, and 6.6% were prepared with reaction conditions as follows: soybean protein isolates concentration of 5% (w/v), glutaminase addition level of 400 U/kg soybean protein isolates, reaction temperature of 37°C, and reaction times of 12, 24, and 36 h, respectively. SDS-PAGE and size exclusion chromatography analysis showed that glutaminase exhibited weak ability to catalyze the hydrolysis of the peptide bonds in soybean protein isolates. The results indicated that the deamidated soybean protein isolates prepared showed improved solubility in a pH range of 3 to 10, and had higher emulsion stability on the oil-in-water dispersions when compared to the original soybean protein isolates, but had poor emulsifying activity. Rheological assay revealed that the suspensions prepared by the deamidated soybean protein isolates products showed higher apparent viscosity, and the values of apparent viscosity depended on the degree of deamidation of the deamidated soybean protein isolates product and the addition level of Ca2+ in the suspensions. The storage modulus G′ and viscous modulus G′′ of the prepared suspensions gave similar behaviors as apparent viscosity. Three deamidated soybean protein isolates products prepared contained better iron (II)-chelating activity than the original soybean protein isolates as the evaluated index showed an increase of 19 to 30%. Limited deamidation of soybean protein isolates by glutaminase showed beneficial impacts on the selected properties of deamidated soybean protein isolates totally, and might be served as a practical approach to prepare multifunctional ingredients for the food industry.
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Plant Foods for Human Nutrition, 1997
Pea (Pisum sativum), faba bean (Vicia faba) and soybean (Glycine max) seeds were characterized, a... more Pea (Pisum sativum), faba bean (Vicia faba) and soybean (Glycine max) seeds were characterized, and protein isolates were prepared following an isoelectric point precipitation procedure. Soybean seeds showed the highest protein content (36.7%) and carbohydrate was the major constituent in the pea (59.4%) and the faba bean seeds (52.1%). Protein contents were higher than 80% in all the protein isolates. The amino acid contents in the protein isolates were, in general, higher than those in their own starting seeds. The antinutritional factor contents were reduced after the protein isolate preparation. The highest reductions achieved for tannins were 95% in the faba bean protein isolate, and for phytates (45%) and trypsin inhibitor activity (46%) in the pea protein isolate. Haemagglutinating activity was not detected in any of the protein isolates. Minimum solubility values were observed at a pH range between 4.0 and 6.0, and maximal solubilities were obtained at basic pH values. The faba bean protein isolate showed the highest water and oil absorption capacities, and the best gelling properties. The soybean protein isolate had the best foam expansion capacity. Thus, the protein isolates had an improvement in some of the characteristics compared to their original seeds with lower contents in tannins, phytates and haemagglutinating activity, but had weak functional properties.
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Food Chemistry, 2010
Protein isolates were analysed from two Mediterranean legumes, Lathyrus clymenum and L. annuus. P... more Protein isolates were analysed from two Mediterranean legumes, Lathyrus clymenum and L. annuus. Protein isolates were prepared by alkaline extraction, including sodium sulphite and acid precipitation of Lathyrus proteins at their isoelectric point (pH 4.5). The percentage of proteins recovered from L. annuus and L. clymenum flours during the preparation of the protein isolates was around 60%. Chemical composition, nutritional parameters, main functional properties and protein composition of Lathyrus protein isolates were studied. L. annuus and L. clymenum protein isolates contained 81.07% and 82.4% of proteins, respectively, and they have a balanced content of essential amino acids, except for sulphur amino acids, with respect to the FAO pattern. The in vitro protein digestibility increased in the protein isolates to 93% and 95% in L. annuus and L. clymenum, respectively. Functional properties were similar to those observed in other legumes protein isolates. These results confirm the interest of local crops as sources of high value protein products obtained after convenient protein extraction procedures and the removal of antinutritional components. These high added value protein isolates are of interest for the food industry and for the revalorisation of L. annuus and L. clymenum favouring the bioconservation of Lathyrus.
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Food Chemistry, 2001
Protein isolates of beach pea were prepared using sodium hydroxide (NaOH) and sodium hexametaphos... more Protein isolates of beach pea were prepared using sodium hydroxide (NaOH) and sodium hexametaphosphate (SHMP). Functional properties of the isolates so prepared were investigated and compared with those of other pea samples. Protein isolate of beach pea, prepared via NaOH extraction, had a protein content of 86.6%, while SHMP-extracted isolates contained 85.1% protein. Corresponding values for NaOH- and SHMP-extracted green pea and grass pea were 90.6, 89.9, 90.6 and 88.3%, respectively. Sulphur-containing amino acids were more prevalent in SHMP-extracted beach pea and green pea, while they were higher in NaOH-extracted grass pea. Tryptophan content was higher in NaOH-extracted than SHMP-extracted isolates. The predicted biological value and protein efficiency ratio of beach pea protein isolates indicated the high quality of products so prepared. Beach pea protein isolates exhibited a minimum solubility at pH 4.5. The pH and NaCl concentration effectively changed the functional properties of protein isolates. Beach pea protein isolates (NaOH- and SHMP-extracted) had in-vitro digestibility of 80.6 to 82.6% for pepsin-trypsin and 78.6 to 79.2% for pepsin-pancreatin.
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Food Chemistry, 2007
Oat bran protein concentrate (OBPC) was prepared from oat bran, and hydrolyzed using trypsin. Pro... more Oat bran protein concentrate (OBPC) was prepared from oat bran, and hydrolyzed using trypsin. Protein hydrolysates of three different degrees of hydrolysis (4.1%, 6.4% and 8.3% respectively) were obtained. SDS-PAGE analysis demonstrated that oat globulin was the major protein component in OBPC. After trypsin treatment, acidic polypeptides were partly degraded into large peptides (Mr=29,000–33,000) and small peptides (Mr<20,000); however, basic
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Food Research International, 1998
Commercial defatted soy meal was solubilized in an aqueous solution at pH 8.5 to prepare a soy pr... more Commercial defatted soy meal was solubilized in an aqueous solution at pH 8.5 to prepare a soy protein isolate (SPI) with 90.45% protein and 95% solubility. Soy protein hydrolysate (SPH) was obtained by enzymatic hydrolysis of the SPI using a neutral proteinase at different degrees of hydrolysis (DH=4, 6, 8 and 10). A previous heat treatment of native SPI at
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Canadian Institute of Food Science and Technology …, 1983
ABSTRACT
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Food and Bioprocess Technology
The physicofunctional and chemical properties of acid-aided protein isolate (AcPi), alkaline-aide... more The physicofunctional and chemical properties of acid-aided protein isolate (AcPi), alkaline-aided protein isolate (AlPi) and soy protein isolate (SPI) prepared from tilapia muscle and defatted soy flour as a function of pH and/or NaCl concentration were investigated. Both acid- and alkali-aided processes lead to significant recoveries (P < 0.05) of proteins with substantial reduction of lipids in AlPi (0.81%) and AcPi (0.96%), the lowest for SPI (0.336%) facilitated by the processing method and sample used. There is greater lipid reduction at alkali pH, effective removal of impurities such as bones and scales, indicated by percentage ash (AcPi, 4.53%; AlPi, 3.75% and SPI, 3.51%). No major difference noted in sodium dodecyl sulphate polyacrylamide gel electrophoresis protein bands (14.4–97.4 kDa) possibly representing partial hydrolysis of myosin. Solubility was the highest at pH 3.0 and 11.0 and the lowest at isoelectric point with foam capacity showing similarity at varying pH. The addition of NaCl improved foam stability, possibly due to the increased solubility and surface activity of the soluble protein. On the whole, AcPi, AlPi and SPI manifested lower solubility and foamability at pH 4.0 and 5.0. AlPi exhibited appreciable levels of solubility, emulsion capacity, oil-holding capacity, viscosity and whiteness, whereas SPI had appreciable water-holding capacity. AcPi, AlPi and SPI have excellent relevance for product development based on their functionality.
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Food Chemistry, 2009
... Leila Mirmoghtadaie a , Mahdi Kadivar Corresponding Author Contact Information , a , E-mail T... more ... Leila Mirmoghtadaie a , Mahdi Kadivar Corresponding Author Contact Information , a , E-mail The Corresponding Author and Mohammad Shahedi a. ... This finding does not agree with those reported by (Lawal, 2005), (El Adawy, 2000) and (Lawal et al., 2007) on Lablab bean ...
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Journal of Agricultural and Food Chemistry, 1999
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