• Asian-Australasian Journal of Animal Sciences
• /
• v.8 no.2
• /
• pp.135-138
• /
• 1995

Soybean meal was fermented by Aspergillus usami in order to reduce phytate content. Aflatoxin B1 was not detected in the fermented soybean meal. The contents of crude protein, crude fiber, ether extract and crude ash were slightly increased following fermentation with a concomitant reduction in nitrogen free extract. Though the fermentation partly degraded proteins in the soybean meal, there was small difference in amino acid composition between the soybean meal and the fermented soybean meal. The results showed that the fermentation did not affect nutritional value of protein in soybean meal. Approximately 55% of phosphorus extracted by trichloroacetic acid was inositol hexaphosphate (phytate) in the soybean meal. The content of inositol tetra to hexaphosphates was not detected in the fermented soybean meal. These results indicated that the fermentation almost completely eliminated phytate in soybean meal. Phytase activity was not detected in the unfermented soybean meal. However, the enzyme activity in the fermented soybean meal was 167.7 U/g. When the fermented soybean meal in supplemented in formula feeds, phytase in the fermented soybean meal might partly degrade the phytate in other ingredients in the digestive tract. The fermented soybean meal is possibly used as a phytate-free protein source of feed, which contains high available phosphorus.

• Nutritional Sciences
• /
• v.9 no.4
• /
• pp.317-322
• /
• 2006

Soybeans are well-known as allergenic foods. Koreans consume large amounts of soybean foods, such as kochujang, which have gone through the fermentation process. To lower the allergenicity of these foods, we prepared hypo allergenic kochujang with aloe extract (AK). A sensory evaluation was conducted along with a clinical evaluation that used a double-blind, placebo-controlled food challenge (DBPCFC) test These tests were designed to evaluate the acceptability of the fermented foods. In comparison to normal kochujang (NK), AK elicited a higher sensory test score, and the rate of positive reactions in atopic dermatitis patients during the DBPCFC test was reduced. Methods of protein extraction, protein quantitation with sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), and protein identification using two-dimensional (2D) gel electrophoresis were performed for both NK and AK to compare the functional factors. We found a reduction in the levels of high molecular proteins even though the bands of the proteins had not entirely disappeared, indicating that the boiling and fermentation process changed the soybean protein patterns. The rate of the reduction of high molecular proteins was more effective in the AK. In conclusion, AK can be recognized as a food with hypoallergenic effect.

• YAKHAK HOEJI
• /
• v.45 no.3
• /
• pp.293-301
• /
• 2001

Genetically modified organism (GMO) using recombinant DNA technique has been exponentially increased, however there are still arguments for the safety of GM foods. The objective of this research was to compare the allergens of GM soybean(Roundup Ready$^{TM}$) with conventional soybeans. Each soybean extracts were prepared as crude extracts, heated extracts, and as heated and simulated gastric quid (SGF)-digested samples to characterize the stability of allergens to physicochemical treatment. Positive sera from 20 soybean-sensitive patients and control sera from 5 normal subjects were used to identify the endogenous allergens in soybeans. Specific-IgE binding activities to each soybean preparations were evaluated by ELISA and immunoblot technique. In ELISA result, IgE binding activities of positive sera to soy crude extracts generally showed two fold higher mean value than those of control sera, how-ever there was no significant difference between GM soybean and natural soybean varieties. Extracted proteins form each of the soybean preparations were separated with SDS-PAGE. The band pattern of GM soybean was very similar to those of natural soybean varieties. Immunoblots for the different soybeans revealed no differences in IgE-binding protein patterns, moreover, disclosed five prominent IgE-binding bands (75, 70, 50, 44 and 34 kDa) in crude extracts, four (75, 70, 44 and 34 kDa) in heated preparations, one (50 kDa) in heated and SGF-digested preparations. These IgE binding bands were consistent with previously reported results on the soybean. These results indicate that GM soybean (Roundup Ready$^{TM}$) is no different from natural soybean in terms of its allergen.gen.

• Korean Journal of Food Science and Technology
• /
• v.21 no.3
• /
• pp.338-344
• /
• 1989

This study was conducted to investigate the mechanism involved with gelation of soybean proteins, 7S and 11S. For the preparations of soybean gels, calsium coagulation and isoelectric point precipitation through the lactic acid fermentation were employed. The textural properties and microstructure of soybean curds were examined by Instron Universal Testing Machine and Scanning Electron Microscope(SEM), respectively. Soybean cheeses were also prepared from soyprotein curds. The characteristics of prepared soybean cheeses were studied by Instron and Sensory evaluation. Microstructure of soybean curds demonstrated by SEM differed markely, postulating that molecular interaction occured in the curds varied with type of protein and coagulative conditions. Textural parameter measured by Instron demonstrated that the curds and the cheeses made through lactic acid fermentation showed higher values in hardness, gumminess and chewiness than those coagulated with $CaCl_2$ 11S PRF could give the curds with higher values in hardness, cohesiveness, springiness, gumminess and chewiness than SPI and 7S PRF Sensory evaluation results showed that soybean cheese made from 11S PRF scored higher values in taste, chewiness, and hardness. However, panels preferred soybean cheese prepared from SPI in color, chewiness and brittleness.

• Applied Biological Chemistry
• /
• v.31 no.4
• /
• pp.361-370
• /
• 1988

To investigate the interaction between whey and soybean protein, thermal changes of component proteins were analyzed by column chromatography and gel electrophoresis. In the Sephadex G-200 chromatography of the mixture treated at above $80^{\circ}C$, the amount of low molecular weight proteins and high molecular aggregates were increased. This implicated that dissociation of 1ls globulin into subunits and the formation of soluble aggregates between these subunits and whey proteins that contain thiol and disulfide groups. These interaction between soy proteins and ${\beta}-lactoglobulin$, ${\alpha}-lactalbumin$, and proteose-peptone 3 were confirmed by gel electrophoresis. Bovine serum albumin, Immunoglobulin-G(H), Lactoferrin, 1ls-subunits(basic and acidic), and subunit of 7s globulin were also considered to interact each other depending on the condition of the salt solutions.

• Applied Biological Chemistry
• /
• v.37 no.5
• /
• pp.379-384
• /
• 1994

Casein or soybean protein was subjected to the reaction with caffeic acid-tyrosinase system at $30{\sim}35^{\circ}C$ pH 6.8 with aeration for 5 hr. The effects of the modified proteins on male Wistar rats were studied by pair-feeding of a cholesterol-free diet for 2 weeks. Significant decrease in protein digestibility for the rats fed with the modified proteins was observed. The feeding of modified protein from casein caused an enlargement of caecum. The concentration of serum cholesterol and triglyceride in the rats fed with modified proteins were mostly unchanged against the rats fed with untreated proteins. These results suggest that the decrease in protein digestibility induced by enzymic browning-reaction did not cause the decrease in concentration of serum cholesterol.

• Journal of Nutrition and Health
• /
• v.26 no.5
• /
• pp.585-592
• /
• 1993

In order to investigate the hypocholesteremic effect of soybean perptides, soybean protein(ISP), casein(CNP), their peptic hydrolyzates fractionated by acid precipitation at different pH's(SHT, SH8, SH6, SH4, CHT, CH5, CH4) and amino acid mixtures of the same composition as the proteins(SAA, CAA) were fed to rats and the concentration of serum cholesterol was measured. Then in vitro digestibility and molecular weight distribution of the peptides by pepticpancreatic hydrolysis was measured by FPLC. The lower the in vitro digestibility of peptides is, the lower the concentration of serum cholesterol becomes(r=0.986) and the higher the ratio of macropeptides is, the lower the concentration of serum cholesterol becomes(r=-0.932) in rats. These results suggest that the in vitro digestibility of peptides has close relationship to the concentration of serum cholesterol in rats and non-digestible meacropeptides or polypeptides especially more than 1 kDa, formed through digestion in gut, may lower the serum cholesterol in rats.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.22 no.2
• /
• pp.226-233
• /
• 1993

Enzymatic hydrolysates of food proteins (defatted soybean cake, egg albumin and casein) were tested for inhibitory activity against angiotensin-I converting enzyme (ACE). Food proteins were hydrolysed with complex enzyme, bromelain, alcalase, $\alpha$-chymotrypsin, trypsin, papain and pepsin by heating method. The hydrolysates obtained from the treatment of complex enzyme and bromelain showed the higher ACE inhibitory activity. ACE inhibitory activity of hydrolysates exhibited a tendency to be increased until 8hrs and increased with increment of concentration. The activity was also stable by heat treatment at 10$0^{\circ}C$ for 20min. Molecular weight of active fraction was about 1, 400 and defatted soybean cake hydrolysate below 1, 400 in case of defatted soybean cake hydrolysate treated with alcalase. Amino acid of the active fractions was abundant in Asp, Glu, Lys, lle, Leu, Ala and Val.

• Journal of Applied Biological Chemistry
• /
• v.63 no.3
• /
• pp.189-195
• /
• 2020

The soybean (Glycine max L.), also known as the soya bean, is an economically important legume species. Pathogens are always major threats for soybean cultivation. Several pathogens negatively affect soybean production. The soybean is also known as a susceptible host to many viruses. Recently, we carried out systematic analyses to identify viruses infecting soybeans using soybean transcriptome data. Our screening results showed that only few soybean transcriptomes contained virus-associated sequences. In this study, we further carried out bioinformatics analyses using a soybean flower bud transcriptome for virus identification, genome assembly, and single nucleotide variations (SNVs). We assembled the genome of Soybean yellow common mosaic virus (SYCMV) isolate China and revealed two SNVs. Phylogenetic analyses using three viral proteins suggested that SYCMV isolate China is closely related to SYCMV isolates from South Korea. Furthermore, we found that replication and mutation of SYCMV is relatively low, which might be associated with flower bud tissue. The most interesting finding was that SYCMV was not detected in the cytoplasmic male sterility (CMS) line derived from the non-CMS line that was severely infected by SYCMV. In summary, in silico analyses identified SYCMV from the soybean flower bud transcriptome, and a nearly complete genome of SYCMV was successfully assembled. Our results suggest that the low level of virus replication and mutation for SYCMV might be associated with plant tissues. Moreover, we provide the first evidence that male sterility might be used to eliminate viruses in crop plants.

• Korean Journal of Breeding Science
• /
• v.42 no.5
• /
• pp.502-506
• /
• 2010

Soybean seed possesses about 15 allergenic proteins recognized by IgEs from soy-sensitive human. The allergenic impact of soybean proteins limit its extensive usage in a broad range of processed foods. Soybean protein P34 or Gly m Bd 30k of the cysteine protease family is one of the major allergen of the soybean seed. P34-null soybean, PI567476, was identified among soybean (Glycine max & Glycine soja Sieb. and Zucc) of approximately 16,226 accessions from USDA soybean germplasm screened. Also, for P34 gene (Williams 82; whole genome sequence cultivar) and P34 null gene (PI567476) comparative analysis of sequences listed in the NCBI database showed the presence of a SSLP (Simple Sequence Length Polymorphism) of 4 base pair. So, a SSLP marker was designed to reveal the polymorphism of the locus. In this study, a population of 339 $F_2$ recombinant inbred lines generated by cross between Taekwang (Glycine max) and PI567476 was used to select $F_{2:3}$ plant of a P34 null gene. The result separation rate Taekwang type, heterozygous type and PI567476 type were shown in 85: 187: 67 since single gene is concerned in as the separation rate of 1:2:1 in $X^2{_{0.05}}=5.99$, df=2. In future, selected plant will identify protein level, whether P34 null protein is equal to P34 null gene.