• 한국식품저장유통학회지
• /
• 제31권1호
• /
• pp.64-79
• /
• 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.

• 한국작물학회지
• /
• 제43권2호
• /
• pp.101-104
• /
• 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
• /
• 제18권1호
• /
• pp.60-65
• /
• 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.

• 한국축산식품학회지
• /
• 제44권5호
• /
• pp.1108-1125
• /
• 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
• /
• 제39권2호
• /
• pp.123-126
• /
• 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.

• 한국작물학회지
• /
• 제50권2호
• /
• pp.112-119
• /
• 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
• /
• 제29권5호
• /
• pp.398-404
• /
• 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
• /
• 제28권1호
• /
• pp.62-67
• /
• 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
• /
• 제29권3호
• /
• pp.396-403
• /
• 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
• /
• 제29권4호
• /
• pp.499-509
• /
• 1999

완두 종자에 축적되는 저장물질은 주로 전분과 단백질로서 이러한 저장물질 때문에 고정이나 전자현미경 관찰시료를 제작하기가 쉽지 않다. 따라서 자엽을 얇게 절편을 만들고 효소를 사용하여 단일세포로 분리한 다음 고정하여 관찰하였다. 완두의 저장단백질이 축적되는 단백질 저장 액포는 종자발달의 이른 시기에 기존의 액포를 둘러싸고 발달하게 되므로서 액포는 수축되고 단백질 저장 액포는 점점 발달하여 그 가장자리에 단백질 덩어리가 축적되게 된다. 이와는 별도로 종자발달의 이른 시기에 조면소포체의 내강에 전자밀도가 높은 단백질이 축적되기 시작하여 늦은 시기에 이 소포체의 끝이 부풀어서 구형의 단백과립으로 발달하였다. 완두종자의 저장단백질은 주로 vicilin과 legumin으로서 단백과립에 대한 면역세포화학적 방법으로 확인한 결과 vicilin은 세포질에 발달된 작은 단백과립과 단백질 저장액포의 가장자리에 축적된 단백질 덩어리에 모두 반응하였으나 legumin은 세포질의 단백과립에만 반응하였다. 또한 소포체에 존재하는 단백질인 Bip은 단백질 저장액포에 축적된 단백질 덩어리의 안쪽 가장자리에만 반응하였다. 이는 단백질이 활발하게 축적되고있는 시기에 특징적으로 작용하는 Bip의 기능과 관련되는 것으로 사료된다.