• Preventive Nutrition and Food Science
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• v.8 no.3
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• pp.278-283
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• 2003

Textural properties of tofu manufactured with micronized full-fat soyflour (MFS) were enhanced by the addition of soy protein isolate, whey protein concentrate, chitosan oligosaccharide and mushroom powder. The MFS solution (14.2% solid content) was converted to semi-solid tofu by a two-stage heat treatment with the addition of 4% coagulant mix. The MFS tofu was evaluated by a compression test as well as sensory evaluation. To produce the semi-solid gel (MFS tofu) with reasonably high strength and toughness, the MFS solution with 14.2% solid content and 7.0% protein had to be heat treated at 121$^{\circ}C$ for 3min. The relative toughness of MFS tofu was increased by the addition of SPI, showing a 144% increase. The toughness of MFS tofu prepared with the MFS/SPI mixture was greatly increased by the addition of WPC at the level of 0.7% and the water separation from MFS tofu was greatly reduced. Furthermore, the toughness and strength of MFS/SPI tofu was enhanced by the addition of 0.1% chitosan oligosaccharide and 0.2% mushroom powder. The sensory evaluation of the tofu fortified with SPI, chitosan oligosaccharide and mushroom powder was superior to that of MFS tofu, with a higher score for overall preference.

• Korean Journal of Food Science and Technology
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• v.26 no.4
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• pp.436-441
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• 1994

To investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein isolate (WPI) against rabbit anti ${\alpha}-LA$ antiserum, competitive inhibition ELISA (cELISA) and passive cutaneous anaphylaxis (PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates (WPH) to the antiserum was decreased to $10^{-2.5}-10^{-5.5}$ and less by the hydrolysis. The monovalent antigenicity of the WPH hydrolyzed by trypsin, or protease from Asp. nryzae was much lowered by the pretreatment of heat denaturation. The antigenicity of the WPH hydrolyzed by chymotrypsin, trypsin, or pancreatin was much lowered by the pretreatment of pepsin. Especially, the antigenicity of TDP (trypic hydrolysate with pretreatment of heat and pepsin) was found almost to be removed. However, there was not consistency between degree of hydrolysis(DH) and the monovalent antigenicity of the WPH. By the heterologous PCA it was found that all of the PGPH lost the polyvalent antigenicity regardless of the pretreatments although WPI and ${\alpha}-LA$ had the positive high antigenicity. The results suggested that the peptides derived from ${\alpha}-LA$ in WPH could bind specific antibodies but they could not induce allergy. Therefore, it was elucidated that the allergenicity of ${\alpha}-LA$ in whey protein could be destroyed easily by the enzymatic hydrolysis.

• Korean Journal of Food Science and Technology
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• v.26 no.1
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• pp.74-80
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• 1994

As a preliminary study about the reduction of the antigenicity of whey protein isolate(WPI) by treatment of chymotrypsin, trypsin, pancreatin, and protease from Aspergillus oryzae, the properties and antigenicities of whey protein hydrolysates(WPH) were investigated. When degrees of hydrolysis (DH) were measured by use of trinitrobenzensulfonic acid(TNBS), the DH of the WPH treated by pancreatin or protease from Aspergillus oryzae$(5.05{\sim}11.47)$ were much higher than those of the tryptic or chymotryptic WPH$(15.67{\sim}20.20)$. And the pretreatments of heat$(75^{\circ}C)$, 20 min and/or pepsin resulted in higher DH of WPH, generally. When the molecular distributions of the WPH were determined by high performance size exclusion chromatography(HPSEC), the ratios of polypeptides with molecular weight more than 10kDa ranged from 12% to 36%, and the average molecular weights and the average peptide lengths of the WPH were $4,252{\sim}9,132$ dalton and $38{\sim}83$ amino acids, respectively. And there was no bitter taste in all of the WPH. Results of SDS-PAGE showed that most of intact native proteins were eliminated by the enzymatic hydrolysis but there were a few bands of peptides larger than 14.2 kDa in some WPH. When antigenicity was assayed by competitive inhibition enzyme-linked immunosorbent assay(cELISA), monovalent antigenicity of WPH to rabbit anti-WPI antiserum were lowered to $10^{-1.7}-10^{-4.9}$ times and less by the enzymatic hydrolysis. And the pretreatments of heat and pepsin resulted in the lowest antigenicicy within a group of enzymatic hydrolysis, especially in case of the pancreatic hydrolysate(PDP) whose antigenicity was found almost to be removed.

• Asian-Australasian Journal of Animal Sciences
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• v.22 no.8
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• pp.1209-1223
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• 2009

In this review, the terminology that is used to describe ileal amino acid (AA) digestibilities in piglet feed ingredients is defined. If one accepts that the determination of AA digestibilities should be based on the ileal analysis method, one should consider that ileal digesta contains variable amounts of endogenous crude protein (CP), which originates mainly from digestive secretions, sloughedoff epithelial cells and mucins. The ileal endogenous CP and AA losses are separated into basal ileal endogenous CP and AA losses ($IAAL_{B}$), which are not influenced by the feed ingredient composition, and specific ileal endogenous CP and AA losses ($IAAL_{S}$), which are induced by feed ingredient characteristics such as level and type of fiber and anti-nutritional factors (ANF). Depending how ileal endogenous CP and AA losses are considered in the measurement of CP and AA digestibilities, digestibility values are expressed as apparent (AID), standardized (SID), or true (TID) ileal digestibilities of CP and AA. The main concern associated with the use of AID values in diet formulation for pigs is that they are not additive in mixtures of feed ingredients. Consequently, the concept of standardized ileal CP and AA digestibilities was introduced by correcting AID values for basal ileal endogenous CP and AA losses ($IAAL_{B}$). The correction for both $IAAL_{B}$ and $IAAL_{S}$ yields TID values, however, routine procedures to measure $IAAL_{S}$ are not yet available. In principle, SID values should be preferred, because they represent the fundamental properties of the feed ingredient. There exist only few reports on SID of CP and AA in feedstuffs frequently used in piglet nutrition. These include soybeans (SB), soybean meal (SBM), soy proteins (SP), soy protein concentrate (SPC), soy protein isolate (SPI), corn gluten (CG), wheat gluten (WG), pea protein (PeaP), potato protein (PotP), fish meal (FM) and whey proteins (WP), but the results obtained are inconsistent. Differences in SID values within feed ingredients may, at least in part, be attributed to different processing conditions or inherent differences of the assay feed ingredients. Moreover, there is some evidence that the determination of SID values and $IAAL_{B}$ in piglets may be confounded by the dietary CP level of the assay diet, age and (or) body weight (BW), the level of feed intake or the methodological approach used to determine $IAAL_{B}$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.5
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• pp.556-562
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• 1999

The increasing price of surimi has affected the economical benefits of surimi based food industry, To maintain gel strength in low grade surimi, the optimum formulation adding functional proteins to low grade surimi is required. The objective of this study was to develop the optimum formulation of ingredients in making gels in low grade surimi on the addition of functional non-muscle proteins to low grade surmi by measuring rheological properties of the gels. The rheological qualities of the cooked gels made with A and RA grade surimi on the effects of adding five kinds of starches (potato, wheat, waxy maize, corn and modified corn) and four kinds of functional proteins (bovine plasma protein, dehydrated egg white, soy protein isolate and whey protein concentrate) to the gels were evaluated, The gel styengths at cooking with A and RA grade surimi were decreased with increasing the added starches. The kind of starches added affected little the gel strengths in Rh grade surimi, while potato and corn starches decreased at the least in gel strengths of the gel made with A grade surimi with increasing the concentration of starches. The bovine plasma protein (BPP) significantly increased the gel strength, especially in RA grade surimi, but BPP decreased the whiteness of the gel. Therefore, the optimum content of BPP was up to $2\%$ because of the whiteness of the gels in RA grade surimi, The optimum formulation for the gel with RA grade surimi to satisfy the gel strength of 1000$\times$g and $78\%$ moisture was $40.9\%$ surimi, $9.1\%$ dehydrated egg white (DEW) and $0.9\%$ starch, while that with A grade surimi under the same condition was $37.9\%$ surimi, $6.6\%$ DEW and $3,4\%$ starch.

• Korean Journal of Food Science and Technology
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• v.43 no.3
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• pp.321-328
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• 2011

Edible films were developed from jujube (Zizyphus jujube Miller) using depolymerization processes of ultrasound and high-pressure homogenization. A 4.6% (w/w) jujube hydrocolloid was treated by ultrasound (600W, 20 min) or homogenized at high pressure (172 MPa, 6 s) and mixed with whey protein isolate, glycerol, xanthan, and sucrose esters of fatty acids to form film-forming solutions from which films were formed by drying. The film prepared by highpressure homogenization (HPH film) produced more homogeneous films without particles than those prepared without depolymerization or with the ultrasound treatment. HPH films possessed the highest tensile strength (4.7MPa), the lowest water vapor permeability ($2.9g{\cdot}mm/kPa{\cdot}h{\cdot}m^2$), and the most uniform and dense microstructures among the films. Flavor profiles of jujube powder and the films were distinguishable. Heat seal strength and oxygen permeability of the HPH films were 44.4 N/m and $0.025mL{\cdot}{\mu}m/m^2$/day/Pa, respectively. Antioxidant activities of jujube power and HPH films were not significantly different.

• Korean Journal of Food Science and Technology
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• v.40 no.3
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• pp.303-310
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• 2008

This study was performed to verify the effects of encapsulation against oil oxidation. Thiobarbituric acid (TBA) values of samples were compared during storage at $60^{\circ}C$, indicating that the encapsulated avocado oil had lower TBA values than the free avocado oil. Microcapsules consisting of a whey protein isolate (WPI)-only wall system had slightly improved oxidative stability; however, spray-dried particles containing a high proportion of maltodextrin (MD) clearly offered better protection from oxidation than the other forms of encapsulation. The chlorophyll (Chl) content of the encapsulated avocado oil was higher than that of the free oil sample. When compared to the control, all wall systems protected the change of the chlorophyll content storage. No large differences were observed between the encapsulated powders according to the various wall materials. The color of the encapsulated oil changed from green to yellowish-green, indicating the formation of pheophytin from chlorophyll. The yellowish color of the oil correlated with a reduced total Chl content. In conclusion, encapsulation with spray drying for avocado oil could lead to improved stability during storage with respect to oxidation and the preservation of chlorophyll.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.05a
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• pp.89-119
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• 2004

This study was conducted to isolate lactobacilli having probiotic characteristics to be used as health adjuncts with fermented milk products. Acid tolerant strains were selected in Lactobacilli MRS broth adjusted to pH 4.0 from 80 healthy persons (infants, children and adults). And bile tolerant strains were examined in Lactobacilli MRS broth in which 1.0% bile salt was added. By estimation above characteristics, the strains No. 27, which was isolated from adult feces, was selected and identified as Lactobacillus salivarius subsp. salivarius based on carbohydrate fermentation and 16S rDNA sequencing. It was used as a probiotic strain in fermented milk products. The pH of fermented milk decreased from pH 6.7 to 5.0 and titratable acidity increased from 0.3% to 1.0% by L. salivarius subsp. salivarius (isolation strain 20, 35, and 37), when incubated for 36 h at $37^{\circ}C$. The number of viable cell counts of fermented milk was maximized at this incubation condition. The SDS-PAGE evidenced no significant change of casein but distinct changes of whey protein were observed by isolated L. salivarius subsp. salivarius for titratable acidity being incubated by $0.9{\sim}1.0%$ at $37^{\circ}C$. All of the strains produced 83.43 to 131.96 mM of lactic acid and 5.39 to 26.85 mM of isobutyric acid in fermented products. The in vitro culture experiment was performed to evaluate ability to reduce cholesterol levels and antimicrobial activity in the growth medium. The selected L. salivarius subsp. salivarius reduced $23{\sim}38%$ of cholesterol content in lactobacilli MRS broth during bacterial growth for 24 hours at $37^{\circ}C$. All of the isolated L. salivarius subsp. salivarius had an excellent antibacterial activity with $15{\sim}25$ mm of inhibition zone to E. coli KCTC1039, S. enteritidis KCCM3313, S. typhimurium M-15, and S. typhimurium KCCM40253 when its pH had not been adjusted. Also, all of the isolated L. salivarius subsp. salivarius had partial inhibition zone to E. coli KCTC1039, E. coli KCTC0115 and S. enteritidis KCCM3313 when it had been adjusted to pH 5.7. The selected strains were determined to have resistances of twelve antibiotic. Strains 27 and 35 among the L. salivarius subsp. salivarius showed the highest resistance to the antibiotics. Purified ${\alpha}$-galactosidase was obtained by DEAE-Sephadex A-50 ion exchange chromatography, Mono-Q ion exchange chromatography and HPLC column chromatography from L. salivarius subsp. salivarius 27. The specific activity of the purified enzyme was 8,994 units/mg protein, representing an 17.09 folds purification of the original cell crude extract. The molecular weight of enzyme was identified about 53,000 dalton by 12% SDS-PAGE. Optimal temperature and pH for activity of this enzyme were $40^{\circ}C$ and 7.0 respectively. The enzyme was found to be stable between 25 and $50^{\circ}C$. ${\alpha}$-galactosidase activity was lost rapidly below pH 5.0 and above pH 9.0. This enzyme was liberated galactose from melibiose, raffinose, and stachyose, and also the hydrolysis rate of substrate was compound by HPLC. These results indicated that some of the L. salivarius subsp. salivarius (strain 27 and 35) are considered as effective probiotic strains with a potential for industrial applications, but the further study is needed to establish their use as probiotics in vivo.