• Food Science and Preservation
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• v.24 no.1
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• pp.145-152
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• 2017

In this study, near infrared (NIR) spectroscopy known as a non-destructive analysis technique was applied to investigate peptide cleavage and consequent release of amino acids in soybean lumps as affected by its moisture content and incubation time during fermentation at 25 for 3 weeks. The NIR spectra of the soybean lump semi-dried and soaked in saline water showed that absorption intensity around 1,400 nm originating from hydrogen bonds of water decreased and absorption band shifted to 1,430 nm as moisture content decreased during incubation at 25 for 3 weeks. In addition, absorption around 2,050 nm which was assigned to amino groups increased as incubation time increased. NIR spectra data from 1,000 to 2,250 nm showed higher accuracy in the discriminant analysis between outside and inside parts of fermented soybean lumps than visible spectra result. NIR spectroscopy for the amino acid and moisture contents in traditional fermented soybean lumps showed relatively good accuracy with the multiple correlation coefficient ($R^2$) of 0.91 and 0.81, respectively, and root mean square error of cross validation (RMSECv) of 0.23 and 0.83%, respectively, in partial least square regression (PLSR). These results indicate that NIR spectral observations could be applicable to control the fermentation process for preparation of soybean products.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.1
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• pp.115-120
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• 2006

To convert the soybean curd residue (SCR) to functional food ingredient, alkaline fermentation of SCR was performed by Bacillus firmus NA-1 and Bacillus subtilis GT-D for 22 hr at $42^{\circ}C$. The micronized full-fat soy flour (MFS) was fortified to reduce the moisture content as well as to supply protein source. The mucilage and flavor productions in the fermented SCR were enhanced by the fortification of $20\%$ MFS. The peptide production from the SCR fermented with B. subtilis GT-D substantially increased when judged by the detectable amount of tyrosine $(480\;mg\%)$. The production of fibrinolytic enzyme was increased by the fermentation for 22 hr, indicating the relative activity of $62\%$ (B. firmus NA-1) and $47\%$ (B. subtilis GT-D), respectively. The SCR fermented by B. firmus NA-1 and B. subtilis GT-D indicated the consistency of $1.95\;Pa{\cdot}s^n\;and\;0.21\;Pa{\cdot}s^n$, respectively. After freeze-drying, the protease activity (615 unit/g) and a-amylase activity (180 unit/g) were obtained from SCR fermented by Bacillus firmus NA-1 and Bacillus subtilis GT-D, respectively.

• Journal of Microbiology and Biotechnology
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• v.9 no.4
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• pp.509-513
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• 1999

The molecular size reduction and the formation of bitterness during a tryptic hydrolysis of soybean 11S glycinin were determined by using quantitative analysis and organoleptic evaluation. The 11S glycinin of 90% purity was prepared by cryoprecipitation and Con A Sepharose 4B affinity chromatography, and hydrolyzed with trypsin in a pH-stat reactor for 4 h. Bitterness was formed within 1 h of hydrolysis, and then slowly increased up to $3.5\times10^{-5}$ M quinine-HCl equivalent. The extent of hydrolysis (DH) was 7% at 1 h and increased up to 12% by the end of the reaction. The -amino nitrogen content increased from an initial 0.7 mM to 7 mM at the end of the period. The SDS-PAGE analysis showed that the acidic subunit of 11S glycinin was mostly hydrolyzed. The GP-HPLC analysis indicated that the bitterness was mainly contributed by the peptide fractions of molecular weights of 360-2,100 Da.

• Animal Bioscience
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• v.35 no.12
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• pp.1892-1903
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• 2022

Objective: A series of experiment were conducted to evaluate the effects of replacing a part of soybean meal (SBM) at 6% of broiler diets with fermented soybean meal (FSBM) obtained by single or two-stage fermentation by measuring growth performance, antioxidant activity in the jejunum and distal intestinal microflora. Methods: Soybean meal samples were prepared by single-stage fermentation using Bacillus velezensis (Bv) (FSBM_B), or Lactobacillus spp. (as commercial control) (FSBM_L). Additional SBM sample was prepared by two-stage fermentation using Bv and subsequently using Lactobacillus brevis ATCC 367 (Lb) (FSBM_B+L). Enzyme activity, chemical composition, trichloroethanoic acid-nitrogen solubility index (TCA-NSI) and antioxidant activity were measured. Then, in an in vivo study, 320 Ross308 broilers were divided into four groups with ad libitum supply of feed and water. Four groups were fed either a corn-soybean meal diet (SBM), or one of fermented SBM diets (FSBM_B+L, FSBM_B, and FSBM_L). Growth, serum characteristics, microflora, and the mRNA expression of selected genes were measured. Results: Compared to SBM, FSBM_B+L contained lower galacto-oligosaccharide, allergic protein, and trypsin inhibitor, and higher TCA-NSI by about three times (p<0.05). Reducing power and 1,1-diphenyl-2-picrylhydrazyl free radical scavenging ability correlated positively with the TCA-NSI content in FSBM. Growth performances were not significantly different among four groups. In jejunum of 35-day-old broilers, partial replacement of SBM by FSBM_B+L increased the activity of superoxide dismutase and catalase (CAT), and the FSBM_B group had the highest catalase activity (p<0.05). Partial replacement of SBM by FSBM increased relative mRNA expressions of nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), and peptide transporter 1 (PepT1) (p<0.05); however, FSBM_B+L increased CAT mRNA level to 5 times of the control (p<0.05). Conclusion: Using Bv- and Lb-processed SBM through two-stage fermentation to partially replace 6% of diets will improve the gut's antioxidant activity under commercial breeding in broilers.

• Preventive Nutrition and Food Science
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• v.9 no.2
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• pp.138-143
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• 2004

Soybean curd residues (SCR) obtained from hot and cold manufacturing processes were fermented by indigenous microorganisms, Lactobacillus rhamnosus LS and Bacillus firmus NA-l for 15 h at 37$^{\circ}C$. The pH, acidity, viable cell counts, and tyrosine content were evaluated in samples with variations in sugar, starter and type of SCR. The raw Doowon SCR (D-SCR, cold-processed) fermented by indigenous microorganism had a 0.9% acidity and 6.7 ${\times}$ 10$^{7}$ CFU/g viable cell counts, compared with the 0.11 % acidity and 6.7 ${\times}$ 10$^{6}$ CFU/g viable cell counts of raw fermented Pulmuwon SCR (P-SCR, hot-processed). After fermentation of raw P-SCR with 1 % glucose and 1 % L. rhamnosus LS starter, the viable cell counts, tyrosine content and acidity were 4.7 ${\times}$ 10$^{8}$ CFU/g, 16.3 mg% and 0.9%, respectively. In addition, the raw P-SCR fermented with Bacillus firmus NA-l as co-starter had a 0.45% acidity, 2.4 ${\times}$ 10$^{8}$ CFU/g lactic acid bacteria, and 3.3 ${\times}$ 10$^{6}$ CFU/g Bacillus sp. In particular, the tyrosine content was increased 5 fold. The drying of fermented SCR was completed by hot-air drying (5$0^{\circ}C$) within 12 h; the dried P-SCR and D-SCR had 1.8 ${\times}$ 10$^{7}$ CFU/g and 5.3 ${\times}$ 10$^{6}$ CFU/g viable cell counts, respectively. The concentrate of methanol extract from fermented D-SCR inhibited the initial cell growth of E. coli, Staphylococcus aureus and Pseudomonas aeruginosa in liquid culture.

• Korean Journal of Microbiology
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• v.45 no.2
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• pp.185-192
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• 2009

Chungkookjang fermenting Bacillus subtilis 028-1 strain suppressed the growth of Staphylococcus sp. LS2, Saccharomyces cerevisiae, and Candida albicans. B. subtilis 028-1 strain produced antibiotic effectively in the medium of 2% soybean meal and 1% maltose as a disaccharide, when the shaking was continued 15~18 h and the pH of culture medium was maintained under 6.5. The antibiotic activity was optimized when the initial pH of the culture medium of test strain was adjusted with weak alkali, was remained after 20 min of boiling and for more than 1 month in room temperature, and was weakened slowly by the digestion of chymotrypsin and papain. The molecular weight of the antibiotic was identified between 500 and 1,000 dalton by dialysis, and antibiotic substance was considered as not surfactin but a member of iturin family because of the absence of fibrinolytic activity.

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

• Applied Biological Chemistry
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• v.12
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• pp.19-24
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• 1969

As a one of the new methods for soybean protein food processings, an attempt was made to decompose steamed soybean protein to amino acids, peptides, and other water soluble forms by the use of protease produced by Aspergillus sojae, and extract them to use as additives of low protein foods or weaning-foods of children. In this paper, as a one part of this subject, the optimum condition, such as optimum pH, temperature, digestion period, raw material's mixing ratio with wheat meal, amount of water added, and effect of sodium chloride addition, to decompose and extract soybean protein were studied. They were obtained when mixing raw materials with wheat meal in the ratio of 10:4 and adding six folds of water at $40-45^{\circ}C$, pH 5-8 for 18 hrs. digestion. Although sodium chloride addition exerted an unfavorable influence upon the decomposition of the aforementioned materials, it was effective to prolongation of digestion period. Under the abovementioned optimum conditions, the maximum extractability of soybean protein as forms of amino acids, peptides, and other water soluble forms, was nearly 70 percent against protein content of raw materials.

• BMB Reports
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• v.30 no.3
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• pp.173-176
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• 1997

We isolated a cDNA clone that encodes a ribulose-1,5-bisphosphate carboxylase small subunit (rbcS) from spinach using a soybean rbcS cDNA as a probe. The small subunit consists of 180 amino acids including a transit peptide of 57 residues. Comparison of the amino acid sequence with those of other plant species shows a maximum of 70-80% identical residues. Southern blot analysis suggests the existence of multiple rbcS genes in the spinach genome. Northern blot analysis indicates that the rbcS gene is expressed predominantly in leaves and that the expression of the gene is induced by light.

• YAKHAK HOEJI
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• v.56 no.3
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• pp.191-197
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• 2012

We previously reported that the novel isoflavone-free peptide mixture (black soybean peptide, BSP) had several beneficial effects like antiobesity and hypotriglyceridemic effect. However, there are no reports for BSP on anti-hypertensive activity. BSP induced heme oxygenase-1 (HO-1) in HUVECs, thus investigated the HO-1-induced activity in HUVECs and the anti-hypertensive effects in SHR animal model. BSP significantly induced HO-1 expression both at transcriptional and protein levels in a time- and dose-dependent manner as measured by RT-PCR and Western blot analysis, respectively. These inductions were abolished by pretreatment of N-acetyl-cystein (NAC, 1~10 mM), but not by employing Tempol, a superoxide dismutase (SOD) mimetic (1~5 mM). As expected, enzymatic activity (~2 fold) determined by bilirubin formation assay and cGMP concentration (~6 fold) were significantly increased in BSP-treated cells. Based on the numerous evidences on the beneficial effects of HO-1 and our results, we investigated in vivo effects of BSP on the antihypertensive activity. The administration of BSP (1% in drinking water) significantly decreased mean blood pressure (BP) (from $218.6{\pm}6.99$ to $190.0{\pm}3.42$ mm Hg, p<0.01). This result indicates that BSP is strong inducer of HO-1 expression, which may be triggered by oxidative stress, and has anti-hypertensive activity.