• 제목/요약/키워드: in vitro protein digestibility

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Porcine Splenic Hydrolysate has Antioxidant Activity in vivo and in vitro

  • Han, Kyu-Ho;Shimada, Kenichiro;Hayakawa, Toru;Yoon, Taek Joon;Fukushima, Michihiro
    • Food Science of Animal Resources
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    • v.34 no.3
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    • pp.325-332
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    • 2014
  • The antioxidant capacity of porcine splenic hydrolysate (PSH) was studied in vitro and in vivo. Peptide hydrolysates were prepared, using the proteolytic enzyme $Alcalase^{(R)}$. The molecular weights of PSH were 37,666, 10,673, 6,029, and 2,918 g/mol. Rats were fed a 5% (w/v) PSH diet, instead of a casein diet, for 4 wk. The food intake, body weight gain, and liver weight of rats in the PSH group were similar to those in the control (CONT) group. There were no differences in the serum total cholesterol, triglyceride, total protein, or albumin levels between PSH and CONT groups. However, the level of in vivo hepatic lipid peroxidation in PSH group was significantly lower than that in CONT. In vivo hepatic catalase and glutathione peroxidase activities in the PSH group were significantly higher than those in the control group. The in vitro protein digestibility of PSH was lower than that of casein. The in vitro trolox equivalent antioxidant capacity of PSH was significantly higher than that of the peptide hydrolysate from casein. The in vitro radical scavenging activities of PSH were significantly higher than those of the peptide hydrolysate from casein. The present findings suggest that porcine splenic peptides improve the antioxidant status in rats by enhancing hepatic catalase and GSH-Px activities, and indicate a potential mechanism of radical scavenging activity during gastrointestinal passage.

Food Quality and Shelf-life of Korean Commercial Fried Kamaboko (시판어묵의 식품학적 품질과 저장안정성)

  • Ryu, Hong-Soo;Choi, Nam-Do;Lee, So-Yeon
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.47 no.3
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    • pp.211-219
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    • 2014
  • To confirm the food quality and storage stability of commercial Korean kamaboko, we experimented with the composition and textural properties using various surimis and kamaboko products. We also investigated changes in protein digestibility and lipid oxidation of vacuum packed products under chilled storage at $4{\pm}1^{\circ}C$. Among the fish meatbased surimi, vegetable mixed surimi had the lowest protein content (23.73 %), as compared to other surimi (51.9-73.6%). Siginificant (P<0.05) differences in protein, lipid content and degree of fat oxidation were noted between the fried kamaboko products of three companies. Adhesiveness, springiness, cohesiveness, gumminess, chewiness and resilience were similar in all samples, but there were notable differences in hardness and fractuability between samples. In vitro protein digestibility and trypsin indigestible substrate (TIS) were not inversely proportional in fried kamaboko products. The protein digestibility (80.30%) of steamed vegetable mixed fried kamaboko was lower than that of other fried samples (84.9-86.2%). Computed protein efficiency ratio (C-PER) of companies A and C's fried kamaboko was 2.6 but company B's was 1.9. There was no noticeable change in thiobarbituric acid reactive substances (TBARs) or protein digestibility for any of the vacuum packed fried kamaboko during 30 days of chilled storage.

Effect of Phytate on the Solubility and Digestibility of Rapeseed Protein Isolate (분리 유채단백의 용해도와 소화율에 미치는 Phytate의 영향)

  • Cho, Hee-Kyung;Yoon, Jae-Young;Lee, Su-Rae
    • Korean Journal of Food Science and Technology
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    • v.24 no.3
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    • pp.279-283
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    • 1992
  • This study was undertaken to investigate the effects of added phytate and pH on the solubility and in vitro digestibility of low-phytate rapeseed protein isolate. Phytate content of low-phytate rapeseed protein isolate was 1.5%, as a result of 66% removal from defatted rapeseed flour and the protein: phytate ratio was 58:1. Solubility of rapeseed protein isolate at pH 2.0 and pH 11.5 was much higher than near the isoelectric point, pH 5.0. It's solubility was lowered by adding an increased amount of phytate especially at pH 2.0. The inhibitory effect of phytate toward pepsin digestibility of rapeseed protein isolate decreased by the increasing amount of phytate added. It is suggested that the production of low-phytate rapeseed protein isolate is necessary to improve the functionality and nutritional value in order to utilize it as food material.

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Changes in Allergenicity and Digestibility of Egg and Milk by Heat Treatment (가열처리에 따른 우유와 달걀의 Allegenicity의 변화와 소화율에 관한 연구)

    • Journal of the East Asian Society of Dietary Life
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    • v.11 no.2
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    • pp.104-111
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    • 2001
  • The first purpose of this study was to determine the changes in the allergenicity of milk and egg with heat treatment. The allergenicity of milk and egg is known to have a strong antigen. The second purpose of this study was to observe changes of disestibility of milk and egg after heat treatment. For this study, passive cutaneous anaphylaxis(PCA) inhibition experiment by using guinea pig and nonprotein nitrogen(NPN)experiment were attempted. The result were following: 1. The allergenicity of both milk and egg was reduced by heat treatment. 2. The degree of hydrolysis and PCA inhibition increased with longer heating time. 3. The increse in both the degree of hydrolysis and PCA inhibition of milk was higher than that of egg. 4. Egg contained a greater amount of allergen than milk after heat treatment. 5. The digestibility of both milk and egg was reduced by heat treatment. 6. The digestibility was reduced further by increasing heating time. 7. The digestibility of egg was lower than that of milk after the treatment.

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Evaluation of Mulberry (Morus alba) as Potential Feed Supplement for Ruminants: The Effect of Plant Maturity on In situ Disappearance and In vitro Intestinal Digestibility of Plant Fractions

  • Saddul, D.;Jelan, Z.A.;Liang, J.B.;Halim, R.A.
    • Asian-Australasian Journal of Animal Sciences
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    • v.18 no.11
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    • pp.1569-1574
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    • 2005
  • The in situ nylon bag degradation and in vitro intestinal digestibility of dry matter (DM), and crude protein (CP) of mulberry (Morus alba) plant fractions was studied at four harvest stages, 3 (W3), 5 (W5), 7 (W7) and 9 (W9) weeks. Degradability of DM and CP of the whole plant and stem fractions declined significantly (p<0.01) with advancing plant maturity in the order W3>W5 and W7>W9 and W3>W5>W7>W9, respectively. The degradation of DM and CP of the leaf fraction was also influenced by plant maturity but no trend was observed. The degradation of DM and CP of the whole plant and leaves increased rapidly during the first 48 and 24 h of incubation, respectively, when maximum degradation was reached. In vitro intestinal digestibility of CP was more influenced by the residence time in the rumen than by plant maturity. This study showed that mulberry is suitable as a supplement, particularly to low-quality roughages, in providing a source of rapidly available nitrogen to the rumen microbes, hence improving the roughage degradability and intake.

Studies for Physicochemical and In Vitro Digestibility Characteristics of Flour and Starch from Chickpea (Cicer arietinum L.)

  • Chung, Hyun-Jung
    • Preventive Nutrition and Food Science
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    • v.16 no.4
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    • pp.339-347
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    • 2011
  • Flour and isolated starch from chickpea (desi type, 328S-8) were evaluated for their in vitro digestibility and physicochemical properties. The protein content, total starch content and apparent amylose content of chickpea flour and isolated starch were 22.2% and 0.6%, 45.8% and 91.5%, and 11.7% and 35.4%, respectively. Chickpea starch granules had an oval to round shape with a smooth surface. The X-ray diffraction pattern of chickpea starch was of the C-type and relative crystallinity was 24.6%. Chickpea starch had only a single endothermic transition (13.3 J/g) in the DSC thermogram, whereas chickpea flour showed two separate endothermic transitions corresponding to starch gelatinization (5.1 J/g) and disruption of the amylose-lipid complex (0.7 J/g). The chickpea flour had a significantly lower pasting viscosity without breakdown due to low starch content and interference of other components. The chickpea starch exhibited significant high setback in the viscogram. The average branch chain length, proportion of short branch chain (DP 6~12), and long branch chains (DP${\geq}$37) of isolated chickpea starch were 20.1, 20.9% and 9.2%, respectively. The rapidly digestible starch (RDS), slowly digestible starch (SDS) and resistant starch (RS) contents of chickpea flour and starch were 9.9% and 21.5%, 28.7% and 57.7%, and 7.1% and 9.3%, respectively. The expected glycemic index (eGI) of chickpea flour (39.5), based on the hydrolysis index, was substantially lower than that of isolated chickpea starch (69.2).

Changes of Proteolytic Enzyme Property by Gamma Irradiation (감마선 조사에 의한 단백질분해효소의 특성변화)

  • Yook, Hong-Sun;Lee, Hyun-Ja;Im, Sung-Il;Kim, Sung;Byun, Myung-Woo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.26 no.6
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    • pp.1116-1121
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    • 1997
  • Effects of gamma irradiation onf the activity and the properties(amino acid compositions, in vitro digestibility and SDS-PAGE pattern) of proteolytic enzymes were investigated. The proteolytic activity of soluble human serine protease, enzyme in kiwi and pineapple decreased 10% and 30~65% by 5 kGy and 30 kGy, respectively. In dried pancreatin and lysozyme, the proteolytic and antimicrobial activities decreased 6~14% and 10~20% by 5kGy and 40kGy, respectively. The analysis of above 10kGy-irradiated soluble human serine protease by SDS-PAGE revealed radiolysis of the enzyme into protein or peptides of lower molecular weights. The irradiation of skim milk, hammastein casein, and lysozyme up to 40kGy had no deleterious effect on either the in vitro digestibility or amino acid compositions.

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In Sacco Evaluation of Rumen Protein Degradation Characteristics and In vitro Enzyme Digestibility of Dry Roasted Whole Lupin Seeds (Lupinus albus)

  • Yu, P.;Egan, A.R.;Leury, B.J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.12 no.3
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    • pp.358-365
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    • 1999
  • The effects of dry roasting whole lupin seeds (lupinus albus, WLS) at 110, 130 or $150{^{\circ}C}$ for 15, 30 or 45 minutes on the in sacco rumen degradation characteristics, optimal heating conditions of time and temperature and in vitro enzyme digestibility were determined. Ruminant degradation characteristics (RDC) of crude protein (CP) of WLS were determined by in sacco technique in dairy cows. Measure ROC were soluble (S), undegradable (U), potentially degradable (D) fractions, lag time (TO) and rate of degradation (Kd) of insoluble but degradable fraction. Based on measured ROC, percentage bypass CP (%BCP) and bypass CP (BCP in g/kg, DM) were calculated. Degradability of CP was significantly reduced by dry roasting (p<0.001). The interaction of dry roasting temperature and time had significant effects on D (p<0.05), Kd (p<0.01), U (p<0.01), %BCP (p<0.001) and BCP (p<0.001) but not on S (p=0.923>0.05). With increasing time and temperature, S, D, Kd and U varied from 31.8%, 67.4%, 10.3%/h and 0.8% in the raw WLS (RWLS) to 27.1 %, 35.8%, 3.6%/h, 38.4% in $150{^{\circ}C}/45\;min$, respectively. All these effects resulted in increasing %BCP from 25.9 in RWLS to 61.0% in the $150{^{\circ}C}/45\;min$. Therefore BCP increased form 111.2 to 261.2 g/kg DM, respectively. Both %BCP and BCP at $150{^{\circ}C}/45\;min$ increased nearly 2.5 times over the RWLS. The effects of dry roasting on %BCP and BCP seemed to be linear up to the highest value tested. Although ROC had been altered by dry roasting, the In vitro perpsin-cellulase digestibility was generally unchanged. It was concluded that dry roasting was effective in shifting CP degradation from rumen to the lower gastrointestinal tract to potential reduce unnecessary N loss in the rumen. It might be of great value in successfully synchronizing the rhythms of release of nitrogen and energy in the rumen, thus achieving a more efficient fermentation of diets with high proportions of lignocellulosic resources. To determine the optimal dry roasting conditions, the digestibility of each treatment in the cows will be measured in the next trial using mobile bags technique.

High Temperature-Cooking Effects on Protein Quality of Fish Extracts

  • Ryu, Hong-Soo;Moon, Jeong-Hae;Hwang, Eun-Young;Yoon, Ho-Dong
    • Preventive Nutrition and Food Science
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    • v.3 no.3
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    • pp.241-247
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    • 1998
  • Fish extracts were processed at high temperature (136.7 ~14$0^{\circ}C$) for possible use as functional food ingredients. Raw fish meats and those hydrothermal extracts were compared with respect to in vitro and in vivo protein qualities. 95% of fat inraw meats was reduced in extracts but there were not remarkable changes in other macronutrients in freeze-dried extracts. Most of essential amino acids were decreased significantly but two times more proline and glycine were detected in extracts. High temperature cooking resulted 2.1 ~3.7 times of higher total free amino acid content infish extracts compared iwth raw meat, and taurine and glutamic acid were increased especially. Severe protein damages were occurred when invitro protein quality indices such as availblae lysine, hydrophilic browing, trypsin inhibitor formation and in vitro protein digestibility were measured on fish extracts. In vivo protein qualities were also strongly influenced by high temperature ; however rat-body-weight gain was nearly zero during PER assay, and rat PER or NPR of fish extracts were significantly lower (p<0.001) than those of cotnrol (ANRC casein) and original raw fish meats.

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Protein Quality Evaluation of Cooked Monkfish (Lophiomus setigerus) Meats

  • Jeung Young-Ae;Ryu Hong-Soo;Shin Eun-Soo;Mun Sook-Im
    • Fisheries and Aquatic Sciences
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    • v.6 no.4
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    • pp.165-171
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    • 2003
  • To investigate the effect of cooking methods on protein quality of domestic fresh monkfish meat (FMM) and imported frozen monkfish meat (IMM), in vitro protein qualities were determined by amino acid anlysis, trypsin indigestible substrate (TIS) formation, and protein digestibility using the four-enzyme method. Crude protein contents of the boiled FMM and IMM were $90\%$ of the dry base, which were higher than fresh FMM $(82\%)$ and IMM $(84\%)$. Profiles of total amino acid in FMM and IMM were not changed by cooking methods. Total free amino acid contents decreased to $ 29.0-33.6\%$ for boiled $(l00^{\circ}C,\;10 min)\;and\;24\%$ for steamed $(100^{\circ}C,\;10\;min)$ samples. In vitro protein digestibilities of boiled and steamed FMM incnased $86.6-86.8\%$, compared to raw IMM $(82.9\%)$, boiled and steamed IMM $85.1-85.5\%$ and raw IMM $(83.6\%)$. TIS of FMM (23.6 mg/g solid) and IMM (15.9 mg/g solid) showed no significant (p<0.05) difference in cooking methods. The C-PERs (computed protein efficiency ratio) of boiled FMM (2.63) and IMM (2.50) were significantly higher (<0.05) than raw (1.97) and steamed FMM(1.97) and IMM(1.94). These results demonstrate that boiling of FMM and IMM improves protein digestibility and C-PER when compared to steamed FMM and IMM. Therefore, boiling could be an excellent means to maintain high-protein quality of monkfish meat. Also, the cooking method may be applicable to the preparation of monkfish stew without any loss of free amino acids.