• Food Science and Preservation
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• v.31 no.1
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• pp.64-79
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• 2024

The rise in popularity of vegetarian and plant-based diets has led to extensive research into plant-based whipped creams. Whipped cream is an oil-in-water emulsion that creates foam through whipping, stabilizing the foam with proteins and fats. Pea protein is an excellent emulsifier and foaming agent among plant-based proteins, but its application in whipped cream is currently limited. The objective of this study was to investigate the quality characteristics of plant-based whipped cream made with ultrasonicated pea protein. The whipped creams were evaluated based on their quality characteristics. A commercially available dairy whipped cream (CON) was used as a control. Plant-based creams were evaluated using pea protein solution, cocoa butter, and canola oil to produce un-ultrasonicated pea protein whipped cream (PP) and ultrasonicated pea protein whipped cream (UPP) at 360 W for 6 min. UPP significantly reduced whipping time and foam drainage compared with CON and PP, resulting in significantly increased overrun, fat destabilization, and hardness. Optical microscopy showed that UPP had smaller fat globules and bubble size than PP. The fat globules of UPP and CON were mostly below 5 ㎛, whereas those of PP were distributed at 5-20 ㎛. Finally, ultrasonication significantly improved the overrun, foam drainage, fat destabilization, and hardness of UPP, which are significant quality characteristics of whipped creams. Therefore, ultrasonicated plant-based pea protein whipped cream is believed to be a viable alternative to dairy whipped cream.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.43 no.2
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• pp.101-104
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• 1998

This study was conducted to establish a rapid analysis method for determining protein and moisture contents of pea. Ninety and eighty pea (Pisum sativum L.) lines were analyzed to determine protein and moisture contents, respectively using near-infrared reflectance spectroscopy. Simple correlations (${\gamma}$) of protein content in a ground sample and an intact grain sample by an automatic regression method were 0.978 and 0.910, respectively. Simple correlations by partial least square regression/principal component analysis (PLS/PCA) methods were 0.982 and 0.925, respectively. Standard error of performance (SEP) in protein content was the lowest value, 0.446 in ground sample by PLS/PCA methods. Simple correlation of moisture content was the highest at 0.871 in ground samples. when using a standard regression method. Accuracy for the moisture content was slightly lower than for protein content. It was concluded that the NIRS method would be applicable only for rapid determination of protein content in pea.

• Food Science and Biotechnology
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• v.18 no.1
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• pp.60-65
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• 2009

Near infrared reflectance spectroscopy (NIRS) was used as a rapid and non-destructive method to determine the protein content in intact and ground seeds of pea (Pisum sativum L.) germplasms grown in Korea. A total of 115 samples were scanned in the reflectance mode of a scanning monochromator at intact seed and flour condition, and the reference values for the protein content was measured by auto-Kjeldahl system. In the developed ground and intact NIRS equations for analysis of protein, the most accurate equation were obtained at 2, 8, 6, 1 math treatment conditions with standard normal variate and detrend scatter correction method and entire spectrum (400-2,500 nm) by using modified partial least squares regression (n=78). External validation (n=34) of these NIRS equations showed significant correlation between reference values and NIRS estimated values based on the standard error of prediction (SEP), $R^2$, and the ratio of standard deviation of reference data to SEP. Therefore, these ground and intact NIRS equations can be applicable and reliable for determination of protein content in pea seeds, and non-destructive NIRS method could be used as a mass analysis technique for selection of high protein pea in breeding program and for quality control in food industry.

• Food Science of Animal Resources
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• v.44 no.5
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• pp.1108-1125
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• 2024

Cultured meat is under investigation as an environmentally sustainable substitute for conventional animal-derived meat. Employing a scaffolding technique is one approach to developing cultured meat products. The objective of this research was to compare soy and pea protein in the production of hydrogel scaffolds intended for cultured meat. We examined the gelation process, physical characteristics, and the ability of scaffolds to facilitate cell adhesion using mesenchymal stem cells derived from porcine adipose tissue (ADSCs). The combination of soy and pea proteins with agarose and agar powders was found to generate solid hydrogels with a porous structure. Soy protein-based scaffolds exhibited a higher water absorption rate, whereas scaffolds containing agarose had a higher compressive strength. Based on Fourier transform infrared spectroscopy analysis, the number of hydrophobic interactions increased between proteins and polysaccharides in the scaffolds containing pea proteins. All scaffolds were nontoxic toward ADSCs, and soy protein-based scaffolds displayed higher cell adhesion and proliferation properties. Overall, the soy protein-agarose scaffold was found to be optimal for cultured meat production.

• Journal of Plant Biology
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• v.39 no.2
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• pp.123-126
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• 1996

The pattern of seed storage protein, vicilin, deposition and site of intracellular localization was examined in cotyledon cells of pea (Pisum sativum) seed using the immunocytochemical methods. The vicilin was confined to the cisternae fo the rough endoplasmic reticulum and dictyosome as well as protein granules newly formed in rough endoplasmic reticulum. Vacuolar protein deposites and protein bodies were also labelled by gold particles. After small protein bodies were formed in the rough endoplasmic reticulum, they were transported to large protein bodies and then fused together. Electron dense protein granule, elaborated in the dictyosome, appears to be transported from dictyosome to protein body. A few unlabelled protein granules seem to be accumulated in other type of proteins than vicilin.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.50 no.2
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• pp.112-119
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• 2005

The effects of Rhizobium inoculant, nitrogen, phosphorus, and molybdenum on nodulation, dry matter production, yield attributes, pod and seed yields, protein and phosphorus contents in seed of pea (pisum sativum) var. IPSA Motorshuti-3 were assessed by a field experiment. Among the treatments Rhizobium inoculant in combination with 25kg P and 1.5kg Mo/ha performed best in recording number of nodules/plant, total dry matter yield, number of pods/plant, number of seeds/pod, 1000-seed weight, green pod yield, green and mature seed yields of pea. The highest green pod yield of 15.37 t/ha ($97.05\%$ increase over control) and green seed yield of 9.6t/ha ($69.31\%$ increase over control) were obtained by inoculating pea with Rhizobium inoculant in association with 25kg P and 1.5 Mo/ha. The effects of 60 or 120kg N/ha were comparable to Rhizobium inoculant in most cases. There were positive correlations among yield attributes, yield, protein and phosphorus contents in seeds of pea. From the viewpoint of yield attributes, yield, and seed quality, application of Rhizobium inoculant along with 25kg P and 1.5kg Mo/ha was considered to be the balanced combination of nutrients for achieving the maximum output from cultivation of pea in Shallow-Red Brown Terrace Soil of Bangladesh.

• BMB Reports
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• v.29 no.5
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• pp.398-404
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• 1996

Light-chilling effects were investigated in chilling-sensitive cucumber (Cucumis sativus L. cv. Ilmichungjang) and chilling-resistant pea (Pisum sativum L. cv. Giant) leaf discs in relation to possible damage in D1 protein. In both plants, dark-chilling did not cause any noticeable changes in (Fv)m/Fm and lincomycin did not affect the decrease in (Fv)m/Fm caused by light-chilling. This result suggests that the de novo synthesis of D1 protein did not occur actively during light-chilling. In pea light-chilled for 6 h. the decreased (Fv)m/Fm was partly recovered in the dark, and almost complete recovery was observed in the light. In cucumber light-chilled for 3 h. the reduced (Fv)m/Fm decreased further for the initial 2 h recovery process in the light regardless of the treatment of lincomycin and recovered very slowly. In both plant species, the treatment of lincomycin inhibited the recovery process in the light, but did not significantly inhibit the process in the dark. In cucumber leaves pulse-labeled with $[^{35}S]Met$, the labeled band intensities of isolated pigment-protein complexes were almost the same during the 6 h light-chilling, but significant decreases in band intensities were observed during the 3 h recovery period. This result suggests that the irreversibly damaged D1 protein was degraded during the recovery period. However, no noticeable changes were observed in the pea leaves during the 12 h chilling and 3 h recovery period. The polyacrylamide gel electrophoresis of the pigment-protein complexes showed that the principal lesion sites of light-chilling were different from those of room temperature photoinhibition.

• BMB Reports
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• v.28 no.1
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• pp.62-67
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• 1995

Thioredoxin f from pea leaves was purified to homogeneity and characterized. The purification steps involved ammonium sulfate fractionation, heat treatment, Sephadex G-75 and G-50 gel filtration, and hydroxyapatite and DEAE ion exchange chromatography. The monomeric molecular weight of purified pea thioredoxin f determined by SDS polyacrylamide gel electrophoresis was 12,000. The purified protein was active in the presence of reducing agents, such as dithiothreitol, at an alkaline pH (7.8~8.5). It was stable against heat such that more than 40% of its maximum activity remained after treatment at $90^{\circ}C$ for 10 min. Pea thioredoxin f was able to reduce insulin and was specific only to pea chloroplast fructose-1,6-bisphosphatase.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.3
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• pp.396-403
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• 2016

The aim was to determine the relative bioavailability of phosphorus (P) in peas for 21-day old broiler chickens using slope-ratio assay. One hundred and sixty eight male Ross 308 broiler chicks were divided into 42 groups 4 balanced for body weight and fed 7 diets in a completely randomized design (6 groups/diet) from day 1 to 21 of age. The diets were a corn-soybean meal basal diet, and the corn-soybean meal basal diet to which monosodium phosphate, brown- or yellow-seeded pea was added at the expense of cornstarch to supply 0.5% or 1% total phosphorus. Monosodium phosphate was included as a reference, and hence the estimated bioavailability of P in pea cultivars was relative to that in the monosodium phosphate. Birds and feed were weighed weekly and on d 21 they were killed to obtain tibia. The brown-seeded pea contained 23.4% crude protein, 0.47% P, whereas the yellow-seeded pea contained 24.3% crude protein and 0.38% P. Increasing dietary P supply improved (p<0.05) chick body weight gain and tibia ash and bone density. The estimated relative bioavailability of p values for brown- and yellow-seeded peas obtained using final body weight, average daily gain, tibia ash, and bone mineral density were 31.5% and 36.2%, 35.6% and 37.3%, 23.0% and 5.60%, and 40.3% and 30.3%, respectively. The estimated relative bioavailability of p values for brown- and yellow-seeded peas did not differ within each of the response criteria measured in this study. In conclusion, the relative bioavailability of P in pea did not differ depending on the cultivar (brown- vs yellow-seed). However, the relative bioavailability of P in pea may vary depending on the response criterion used to measure the bioavailability.

• Applied Microscopy
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• v.29 no.4
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• pp.499-509
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• 1999

Accumulations of the storage proteins in protein storage vacuole and the differentiation of protein bodies from protein-filled ER in developing pea cotyledons have been investigated using conventional and immunoelectron microscopy. To improve the fixation quality, single cells separated enzymatically from sliced cotyledons were used. At early stages of seed development osmiophilic protein accumulates in rER lumen were observed quite often. This protein-filled ER cisternae were differentiated into cytoplasmic protein bodies at late stage by the process called terminal dilations which have been considered a principal route of the formation of cytoplasmic protein bodies somewhat later in seed maturation. Immunocytochemical labellings of the vicilin and legumin show that presence of vicilin on both of the cytoplasmic PB and PD, but limited presence of legumin only on the cytoplasmic PB at intermediate stage of seed development. Immunogold labellings of Bip, ER retention protein, were observed on the inner periphery of protein deposits in protein storage vacuole. This result was regarded that Bip can recognize and retrieve misfolded protein during active accumulation of storage protein to the PD in PSV.