• Title/Summary/Keyword: Alternative protein

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Recovery and Utilization of Proteins and Lipids from the Washing Wastewater in Marine Manufacture by Isoelectric Point Shifting Precipitation Method;4. Utilization of the Recovered Protein Fractions as the Alternative Feed of Fish Meal. (수산가공공장폐액의 등전점이동 응집처리에 의한 유용성분재회수이용;4. 회수단백질의 어분 대체 사료로서의 이용)

  • Kim, Gwang-Woo;Kim, Ga-Hyeon;Ueo, Myung-Hee;Kim, Ok-Seon;Cho, Soon-Yeong
    • Journal of Life Science
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    • v.18 no.6
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    • pp.832-838
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    • 2008
  • Mackerel water-soluble protein fraction produced by washing the mackerel meat were concentrated by isoelectric point shifting precipitation process, and the concentrates were utilized as the alternative feed of fish meal. In the 1st aquaculture diet experiment for Israel common carp, the feed conversion ratio decreased in proportion to the rise in the percentage of the recovered protein containing a residual lipid, which was added to the fish meal. It was supposed that the low feed efficiency was because of lipid oxidation in the recovered protein fraction. In addition, 2nd aquaculture diet experiment for Israel common carp was conducted after removing the oxidized lipid in the recovered protein fish meal. When a portion of the fish meal was substituted by the recovered protein devoid of the residual lipid, the feed conversion ratio increased in proportion to the amount of the substitute being added to the fish meal. Therefore, the recovered protein fraction of the mackerel washing wastewater from mackerel processing factory could be used as the alternative feed of fish meal.

Continuous Cell-Free Protein Synthesis Using Glycolytic Intermediates as Energy Sources

  • Kim, Ho-Cheol;Kim, Tae-Wan;Park, Chang-Gil;Oh, In-Seok;Park, Kyung-Moon;Kim, Dong-Myung
    • Journal of Microbiology and Biotechnology
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    • v.18 no.5
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    • pp.885-888
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    • 2008
  • In this work, we demonstrate that glycolytic intermediates can serve as efficient energy sources to regenerate ATP during continuous-exchange cell-free (CECF) protein synthesis reactions. Through the use of an optimal energy source, approximately 10 mg/ml of protein was generated from a CECF protein synthesis reaction at greatly reduced reagent costs. Compared with the conventional reactions utilizing phosphoenol pyruvate as an energy source, the described method yields 10-fold higher productivity per unit reagent cost, making the techniques of CECF protein synthesis a more realistic alternative for rapid protein production.

Effects of Tannery Wastes on the Fattening of Growing Cattle, Carcass, and Meat Quality

  • Alam, Jahangir;Hossain, Mufazzal;Beg, Anwarul Haque;Nam, Ki-Chang;Lee, Sang-Suk
    • Food Science of Animal Resources
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    • v.30 no.2
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    • pp.190-197
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    • 2010
  • The present study was conducted to determine the effect of tannery waste protein concentrate (TWPC) on fattening of cattle and the carcass and meat quality, with the aim of replacing the costly commercial protein concentrate (Jasoprot) with a more economical and effective alternative. Twelve young cattle (six male and six female) were fed during the study period on a control diet (T1) with 10% Jasoprot and on two test diets: 5% TWPC + 5% Jasoprot (T2) and 10% TWPC (T3). The test diets significantly affected (p<0.05) live weight gain and profitability compared to the control diet, perhaps due to the increased protein and essential amino acid content, relative to Jasoprot. TWPC was free of aflatoxin. Sensory-evaluated organoleptic scores did not differ among the groups. Chemical composition was normal as other beef and was non toxic especially within recommended chromium level ($1.90{\pm}0.6{\mu}g$) Total lipid contents were higher (p<0.05) in T3, and moisture, ash and crude protein contents were almost similar (p>0.05) among the three groups. It is concluded that TWPC or an equal mixture of TWPC and Jasoprot may be an economic and efficient alternative protein source to Jasoprot in the cattle industry, which minimizes adverse effects on carcass and sensory meat quality.

Echinococcus granulosus Protoscolex DM9 Protein Shows High Potential for Serodiagnosis of Alveolar Echinococcosis

  • Kim, Jeong-Geun;Han, Xiumin;Kong, Yoon
    • Parasites, Hosts and Diseases
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    • v.60 no.1
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    • pp.25-34
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    • 2022
  • Alveolar echinococcosis (AE) caused by infection with E. multilocularis metacestode, represents one of the most fatal helminthic diseases. AE is principally manifested with infiltrative, proliferating hepatic mass, resembling primary hepatocellular carcinoma. Sometimes metastatic lesions are found in nearby or remote tissue. AE diagnosis largely depends on imaging studies, but atypical findings of imaging features frequently require differential diagnosis from other hepatic lesions. Serological tests may provide further evidence, while obtaining reliable AE materials is not easy. In this study, alternative antigens, specific to AE were identified by analyzing E. granulosus protoscolex proteins. An immunoblot analysis of E. granulosus protoscolex showed that a group of low-molecular-weight proteins in the range from 14 kDa to 16 kDa exhibited a sensitive and specific immune response to AE patient sera. Partial purification and proteomic analysis indicated that this protein group contained myosin, tubulin polymerization promoting protein, fatty-acid binding protein, uncharacterized DM9, heat shock protein 90 cochaperone tebp P-23, and antigen S. When the serological applicability of recombinant forms of these proteins was assessed using enzyme-linked immunosorbent assay, DM9 protein (rEgDM9) showed 90.1% sensitivity (73/81 sera tested) and 94.5% specificity (172/181 sera tested), respectively. rEgDM9 showed weak cross-reactions with patient sera from the transitional and chronic stages of cystic echinococcosis (3 to 5 stages). rEgDM9 would serve as a useful alternative antigen for serodiagnosis of both early- and advanced-stage AE cases.

Quality Characteristics of Meat Analogs through the Incorporation of Textured Vegetable Protein and Tenebrio molitor Larvae in the Presence of Transglutaminase

  • Yea-Ji Kim;Jeong Heon Kim;Ji Yoon Cha;Tae-Kyung Kim;Hae Won Jang;Dong-Hyun Kim;Yun-Sang Choi
    • Food Science of Animal Resources
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    • v.44 no.5
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    • pp.1028-1039
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    • 2024
  • Alternative protein sources with greater nutritional value and a lower environmental footprint have recently attracted interest in the production of meat substitutes. However, it is required that these alternatives mimic the texture and structure of meat. This study investigated varying ratios of textured vegetable proteins (TVP) to Tenebrio molitor larvae (brown mealworm; TM) with the addition of transglutaminase (TG) to determine the quality characteristics of these emulsions. The results demonstrated low protein solubility of the emulsions as TVP content increased. Furthermore, when the proportion of TM was high, the TG-treated emulsion had a low pH. Additionally, when there was a high TM ratio to TVP in the TG treatment, the emulsions demonstrated better thermal stability and water holding capacity. Regarding the rheological properties of the emulsion, both the frequency-dependent storage modulus (G') and loss modulus (G'') increased as the proportion of TVP in the emulsion increased with and without the addition of TG. Differential scanning calorimetry analyses demonstrated two protein denaturation peaks in all treatments, with high peak temperatures for both treatments with a high proportion of TM. The hardness and chewiness of the emulsion were highest in the treatment (T6 and T8) with TG, and the gumminess of the emulsion was greatest when TM only or when equal ratios of TVP and TM were treated with TG, respectively. In conclusion, the addition of TM to TVP with TG improves the overall texture of the protein mixture, making it a suitable meat alternative.

Molecular Analysis of Alternative Transcripts of the Equine Cordon-Bleu WH2 Repeat Protein-Like 1 (COBLL1) Gene

  • Park, Jeong-Woong;Jang, Hyun-Jun;Shin, Sangsu;Cho, Hyun-Woo;Choi, Jae-Young;Kim, Nam-Young;Lee, Hak-Kyo;Do, Kyong-Tak;Song, Ki-Duk;Cho, Byung-Wook
    • Asian-Australasian Journal of Animal Sciences
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    • v.28 no.6
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    • pp.870-875
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    • 2015
  • The purpose of this study was to investigate the alternative splicing in equine cordon-bleu WH2 repeat protein-like 1 (COBLL1) gene that was identified in horse muscle and blood leukocytes, and to predict functional consequences of alternative splicing by bioinformatics analysis. In a previous study, RNA-seq analysis predicted the presence of alternative spliced isoforms of equine COBLL1, namely COBLL1a as a long form and COBLL1b as a short form. In this study, we validated two isoforms of COBLL1 transcripts in horse tissues by the real-time polymerase chain reaction, and cloned them for Sanger sequencing. The sequencing results showed that the alternative splicing occurs at exon 9. Prediction of protein structure of these isoforms revealed three putative phosphorylation sites at the amino acid sequences encoded in exon 9, which is deleted in COBLL1b. In expression analysis, it was found that COBLL1b was expressed ubiquitously and equivalently in all the analyzed tissues, whereas COBLL1a showed strong expression in kidney, spinal cord and lung, moderate expression in heart and skeletal muscle, and low expression in thyroid and colon. In muscle, both COBLL1a and COBLL1b expression decreased after exercise. It is assumed that the regulation of COBLL1 expression may be important for regulating glucose level or switching of energy source, possibly through an insulin signaling pathway, in muscle after exercise. Further study is warranted to reveal the functional importance of COBLL1 on athletic performance in race horses.

Controversies on governing the rates of protein evolution

  • Choi, Sun-Shim
    • Interdisciplinary Bio Central
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    • v.1 no.3
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    • pp.11.1-11.5
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    • 2009
  • One of the main issues of molecular evolution is to reveal the principles dictating protein evolutionary rates. A traditional hypothesis posits that protein evolutionary rates are mostly determined by the average functional importance of amino acids in a given protein. Thus the correlations of evolutionary rates with different variables such as PPI, gene essentiality and expression abundance have been studied to test the traditional hypothesis. Recently, mRNA expression abundance among the variables has drawn much attention, not only because it shows relatively strong correlation with protein evolutionary rates, but also because of the controversies surrounding an alternative hypothesis against the traditional one. Here, I will give an overview over the traditional hypothesis, and summarize the different variables that have been found to correlate with protein evolutionary rates. Then I will introduce pros and cons on the two different hypotheses.

Comparisons of Recombinant Protein Expression in Diverse Natural Isolates of Escherichia coli

  • Jung, Yuna;Lim, Dongbin
    • Molecules and Cells
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    • v.25 no.3
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    • pp.446-451
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    • 2008
  • We assessed heterologous protein expression in 64 strains obtained from the Escherichia coli Reference (ECOR) collection, a collection representing diverse natural E. coli populations. A plasmid generating a glutathione S-transferase and plant carbonic anhydrase fusion protein (GST-CA) under the control of the tac promoter was introduced into the ECOR strains, and the quantity of the fusion protein was determined by SDS-PAGE. The foreign protein was generated at various levels, from very high (40 strains, high producers) to very low (six strains, low producers). Immunoblotting showed that the high producers expressed approximately 250-500 times more GST-CA protein than the low producers. The results of semi-quantitative RT-PCR showed that the low producers generated mRNA levels comparable to those of the high producers, thereby suggesting that, at least in this case, inefficient translation is a major cause of the low production. We introduced a different plasmid, which expressed a maltose binding protein and plant guanylate kinase fusion protein (MBP-GK) into the six low producers. Interestingly, five of these expressed MBP-GK at very high levels. Thus, we conclude that the production of a particular protein from an expression vector can vary considerably, depending on the host strain. Strains in the ECOR collection could function as useful alternative hosts when a desired level of protein expression is not obtained from commonly used strains, such as E. coli K12 or B derivatives.

A review of canola meal as an alternative feed ingredient for ducks

  • Wickramasuriya, Samiru Sudharaka;Yi, Young-Joo;Yoo, Jaehong;Kang, Nam Kyu;Heo, Jung Min
    • Journal of Animal Science and Technology
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    • v.57 no.9
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    • pp.29.1-29.9
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    • 2015
  • This review provides an overview of the published data on the canola meal and its suitability for duck as an alternative plant-origin protein source to soybean meal. Canola meal is a legume origin protein source containing comparable amino acid profile to soybean meal and rich in essential minerals and vitamins. Nonetheless, it is known to contain less in energy content than soybean meal. Factors like field conditions and processing methods creates compositional variations among canola meal. Presence of anti-nutritional factors such as phenolic substances, phytate and glucosinolates which are known to reduce growth performance in livestock animals, are the major drawbacks for canola meal to be a competitive plant-origin protein source in the feed industry. This review is focused to address i) nutritional characteristics and feeding value of canola meal for ducks and ii) impacts of feeding canola meal on performances of ducks.

Alternative splicing and expression analysis of High expression of osmotically responsive genes1 (HOS1) in Arabidopsis

  • Lee, Jeong-Hwan;Kim, Soo-Hyun;Kim, Jae-Joon;Ahn, Ji-Hoon
    • BMB Reports
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    • v.45 no.9
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    • pp.515-520
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    • 2012
  • High expression of osmotically responsive genes1 (HOS1), a key regulator of low temperature response and flowering time, encodes an E3 ubiquitin ligase in Arabidopsis. Here, we report characterization of a newly identified splice variant (HOS1-L) of HOS1. Comparative analyses revealed that HOS1-L has a longer 5' nucleotide sequence than that of the previously identified HOS1 (HOS1-S) and that its protein sequence was more conserved than that of HOS1-S in plants. HOS1-L transcripts were spatio-temporally more abundant than those of HOS1-S. The recovery rate of HOS1-S expression was faster than that of HOS1-L after cold treatment. Diurnal oscillation patterns of HOS1-L revealed that HOS1-L expression was affected by photoperiod. An in vitro pull-down assay revealed that the HOS1-L protein interacted with the ICE1 protein. HOS1-L overexpression caused delayed flowering in wild-type plants. Collectively, these results suggest regulation of HOS1 expression at the post-transcriptional level.