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Red blood spot (RBS) commonly found in cooked chicken breast has caused severe economic loss as it is perceived as a sign of undercooked product. The objectives of this study were to investigate the cause of RBS as related to common ingredients used in marination, based on both chicken breast and isolated chicken hemoglobin (Hb) models. The effect of sodium chloride (NaCl), sodium tripolyphosphate (STPP), and glucose on thermal denaturation of Hb was investigated along with the extent of RBS formation in cooked marinated chicken breast. After vacuum tumbling for 65 min and subsequent storage at 4 °C for 20 hr, STPP and glucose were not absorbed into the center of chicken breast. However, Na+ was absorbed after 12 hr storage. The denaturation temperature (Td) of isolated chicken Hb decreased to 65.8 °C in the presence of 1.5 M NaCl, while that of the control was 69.4 °C. STPP at pH 9 decreased Td of Hb to 61.4 °C. The alkaline pH induced by STPP destabilized the Hb structure. RBSs were observed at 100% incidence when cooked to core temperatures of 50 and 70 °C for 1 min. RBSs were completely eliminated at core temperature of 85 °C. The ingredients used during marination appeared to have a minimal effect on RBS formation due to their limited absorption into the chicken breast. The cooking temperature is a major factor governing RBSs, as it directly affects the denaturation of Hb. 相似文献
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Jirawat Yongsawatdigul Penprapha Piyadhammaviboon 《Journal of the science of food and agriculture》2005,85(9):1453-1460
In the absence of microbial transglutaminase (MTGase), the textural properties of lizardfish surimi (Saurida spp) improved when pre‐incubated at 4 and 25 °C for 24 and 4 h, respectively. MTGase optimally catalyzed incorporation of monodansylcadaverine (MDC) into surimi at 40 °C. Addition of MTGase appeared to reduce autolytic activity at 25 and 40 °C, but had no effect on autolytic activity at 65 °C. Breaking force and deformation of lizardfish surimi significantly improved when 0.1 unit MTGase g?1 surimi (1.8 g kg?1) was added and pre‐incubated at either 25 or 40 °C. Textural properties improved concomitant with cross‐linked polymers of myosin heavy chain and tropomyosin, but not actin. Addition of MTGase also improved the storage modulus (G′). The gel network of surimi mixed with MTGase and pre‐incubated at 40 °C readily formed during the pre‐incubation period, while formation of the gel network began at 48.1 °C in the absence of MTGase. Copyright © 2005 Society of Chemical Industry 相似文献
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Abstract: Cell‐associated proteinases from Virgibacillus sp. SK33 isolated from fish sauce fermentation were extracted and characterized. Proteinases were effectively released when washed cells were incubated in 0.3 mg/mL lysozyme in 50 mM Tris‐maleate (pH 7) at 37 °C for 2 h. Major cell‐associated proteinases exhibited molecular mass of 17, 32, and 65 kDa, but only a 32‐kDa proteinase showed strong amidolytic activity toward Suc‐Ala‐Ala‐Pro‐Phe‐AMC. Activity of all cell‐associated proteinases was completely inhibited by phenylmethanesulfonyl fluoride, indicating a characteristic of serine proteinase. In addition, a 65‐kDa serine proteinase was also inhibited by ethylenediaminetetraacetic acid, implying a metal‐dependent characteristic. Optimum activity toward a synthetic peptide substrate was at 50 °C and pH 8 and 11. Proteinases with molecular mass of 17 and 32 kDa exhibited caseinolytic activity at 25% NaCl and activity based on a synthetic peptide substrate increased with NaCl concentrations up to 25%, suggesting their role in hydrolyzing proteins at high salt concentrations. This is the first report of liberated cell‐associated proteinases from a moderate halophile, Virgibacillus sp. Practical Application: The cell‐associated proteinases could be extracted from Virgibacillus sp. SK 33 using lysozyme. The extracted enzyme could be applied to hydrolyze food proteins at NaCl content as high as 25%. In addition, this study demonstrated that not only extracellular but also cell‐associated proteinases are key factors contributing to protein‐degrading ability at high salt environment of Virgibacillus sp. SK 33. 相似文献
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Wanida Janvikul Paweena Uppanan Boonlom Thavornyutikarn Jirawat Krewraing Rujiporn Prateepasen 《应用聚合物科学杂志》2006,102(1):445-451
The effects of chitin, chitosan, and their derivatives on in vitro human blood coagulation and platelet activation were comparatively studied. The coagulation was assessed by the measure of the whole blood clotting time (WHBCT) and plasma recalcification time (PRT). The tested materials were chitin, chitosan, partially N‐acetylated chitosan (PNAC), N,O‐carboxymethylchitosan (NOCC), N‐sulfated chitosan, N‐(2‐hydroxy)propyl‐3‐trimethylammonium chitosan chloride, and SPONGOSTAN® standard (a positive control). The results revealed that the WHBCTs of whole blood mixed with chitin, chitosan, NOCC, or SPONGOSTAN® standard were significantly decreased with respect to that of the pure whole blood (a blank control) (P < 0.05), while the WHBCT value of whole blood mixed with PNAC was not significantly reduced. However, the presence of PNAC significantly lowered the PRT value, similar to the addition of chitin, NOCC, or SPONGOSTAN® standard. Chitosan was found to reduce PRT, but not significantly. In the platelet adhesion and activation studies, the morphology of platelets adherent to the film surfaces of tested materials was examined using a scanning electron microscopic technique. Because of their effective coagulation activites, chitosan, PNAC, and NOCC were further evaluated to determine how platelets behaved when in contact with these film samples for given periods. It was found that NOCC activated platelets most effectively. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 102: 445–451, 2006 相似文献
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Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts 总被引:2,自引:0,他引:2
Chompoonuch WiriyaphanBenjamart Chitsomboon Jirawat Yongsawadigul 《Food chemistry》2012,132(1):104-111
Antioxidant activities of protein hydrolysates from threadfin bream surimi wastes, including frame, bone and skin (FBS) and refiner discharge (RD), were investigated. FBS and RD were rich in Lys, Glu, Gly, Pro, Asp, Leu, His, Tyr and Phe. FBS was hydrolysed to a greater extent than RD regardless of proteinases tested (Virgibacillus sp. SK33 proteinase, Alcalase, pepsin and trypsin). Pepsin-hydrolysed FBS, at a 5% degree of hydrolysis (DH), showed the highest antioxidant activity based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical (0.455 ± 0.054 mg Trolox equivalents/mg leucine equivalents), ferric reducing antioxidant power (FRAP) (0.221 ± 0.005 mM Trolox equivalents) and inhibition of β-carotene bleaching assays. FBS hydrolysates showed higher antioxidant activity based on chemical assays than their RD counterparts. However, FBS and RD hydrolysates protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative damage to a similar extent. Therefore, FBS and RD hydrolysates have a potential as antioxidative neutraceutical ingredients. 相似文献
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The conformational changes and rheological properties of soluble sarcoplasmic proteins isolated from striped catfish (Pangasius hypophthalmus), treated at various pHs (2–12), were investigated. Isoelectric point of striped catfish sarcoplasmic proteins was determined to be pH 5. SDS–PAGE of sarcoplasmic proteins treated at various pHs, showed molecular masses ranging from 11 to 97 kDa. Most sarcoplasmic proteins, regardless of treated pHs, showed a molecular mass of 43 kDa. A decrease in total sulfhydryl content was observed when the pH was shifted away from 6, indicating disulfide formation at pH lower and higher than 6. Gradual increases of S0-ANS and S0-PRODAN were observed as pH increased from 6 to 12, indicating the unfolding of sarcoplasmic proteins during alkaline extraction. DSC thermograms of sarcoplasmic proteins treated at pH 5–9 exhibited an exothermic transition peak, probably due to disulfide bond formation, and/or hydrophobic interactions, which was highly related to the onset temperature of G′ rising. Gel network formation of sarcoplasmic proteins did not take place at extreme pHs (<4 or >9) where proteins were highly charged while the viscoelastic properties of sarcoplasmic proteins were observed at pH 5.5–9. The highest G′ value at 90 °C was observed at pH 5.5 and 8 (P ? 0.05). The gel point, a temperature at which G′ = G″, increased to higher temperature as pH was shifted away from 7. 相似文献
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ABSTRACT: Structural changes and functional properties of threadfin bream (Nemipterus sp.) sarcoplasmic proteins (TB-SP) subjected to various pH conditions (pH 3, 5, 6.3, 9, and 12) after subsequent pH readjustment to pH 7 were investigated. Fourier transform infrared spectroscopy revealed the loss of α-helical and β-sheet structures of TB-SP after being subjected to pH 3 or pH 12 treatments. The extent of structural and conformational changes of TB-SP subjected to pH 3 was greater than alkaline pHs (pH 9, 12) and pH 5, respectively. The water holding capacity of lyophilized TB-SP treated at pH 3 and pH 12 increased about 6.5- and 5.4-fold, respectively, as compared to the crude counterpart. Both acid and alkaline pH treatments increased fat absorption capacity of lyophilized sample about 2-fold, but drastically decreased its solubility. The water soluble fraction of extremely acidic (pH 3→7) and alkaline (pH 12→7) samples exhibited higher oil binding capacity as measured by diphenylhexatriene fluorescence and emulsifying activity. A gel-like structure was formed when water-soluble fraction of crude TB-SP and those subjected to moderate pHs (pH 5, 9) at 2 mg/mL was prepared for the emulsion containing 50% oil (v/v). Functional properties of TB-SP varied, depending on the pH-adjustment process applied. 相似文献
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Siriphon Siriangkanakun Eunice C.Y. Li‐Chan Jirawat Yongsawadigul 《Journal of food science》2014,79(7):C1305-C1314
Sarcoplasmic proteins from 3 fish species were fractionated by 50% to 70% ammonium sulfate precipitation. Lyophilized fractionated sarcoplasmic proteins of threadfin bream (TB‐SP), bigeye snapper (BS‐SP), and yellow croaker (YC‐SP) showed 80% to 92% trypsin inhibitory activity. Trypsin inhibitory activity staining gel electrophoresis revealed bands at 32, 33, 37, 45, 48, and 50 kDa for the 3 species, and a band at 95 kDa was observed for TB‐SP and YC‐SP. Alpha‐1‐antitrypsin with molecular mass of 45 to 50 kDa was identified in YC‐SP by gel‐based liquid chromatography‐tandem mass spectrometry (GeLC‐MS/MS). Other major protein bands appeared on trypsin activity staining included phosphorylase, glyceraldehyde‐3‐phosphate dehydrogenase, and creatine kinase with molecular mass of 95 and 35 to 40 kDa, respectively. But, these 3 proteins did not show true trypsin inhibitory activity. Trypsin inhibitory activity of fractionated sarcoplasmic proteins showed good stability, with >80% activity retained at 60 °C and up to 0.6 M NaCl. TB‐SP showed the highest inhibitory activity against autolysis of washed threadfin bream mince at 65 °C. Addition of 0.5% or 1% TB‐SP improved textural properties of threadfin bream surimi gels preincubated at 37 or 65 °C followed by heating at 90 °C. Therefore, TB‐SP could be a promising protein ingredient for enhancing surimi gel texture. 相似文献
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Chemical and Cellular Antioxidant Activities of Chicken Breast Muscle Subjected to Various Thermal Treatments Followed by Simulated Gastrointestinal Digestion
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Papungkorn Sangsawad Ratana Kiatsongchai Benjamart Chitsomboon Jirawat Yongsawatdigul 《Journal of food science》2016,81(10):C2431-C2438
The effect of thermal treatments on chemical and cellular antioxidant activities of chicken breasts subjected to in vitro gastrointestinal digestion was investigated. Breast of Korat crossbred chicken (KC) and commercial broiler (BR) were cooked under various conditions, namely heating at 70 °C for 30 min (H‐0.5) and 24 h (H‐24), autoclaving (AC) at 121°C for 15 min (AC‐15) and 60 min (AC‐60). Protein digestibility decreased upon the extreme thermal treatment of AC‐60. The H‐0.5 improved metal chelating activity of KC digesta, FRAP, and anti‐liposome oxidation of BR digesta. Digesta of BR/H‐0.5 and KC/AC‐15 at 50 μg/mL exhibited the highest cytoprotective effect against tert‐butyl hydroperoxide (TBHP)‐induced oxidative damage of HepG2 cells. In addition, the KC/AC‐15 digesta at a concentration as low as 12.5 μg/mL inhibited intracellular TBHP‐induced reactive oxyfen species (ROS) production (P < 0.05). Thus, the digesta of KC breasts subjected to AC‐15 provides not only nutritional value but also antioxidant activity at the cellular level. 相似文献