• Journal of Animal Science and Technology
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• 제52권5호
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• pp.435-440
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• 2010

유청단백질농축물(WPC)은 풍부한 단백질 및 다양한 생리활성 물질들을 함유하고 있음으로 식품의 단백질 보충 및 건강 기능성 향상을 위해 식품산업에서 널리 사용되고 있는 유용한 식품소재 중에 하나이다. 본 연구는 유용 기능성 식품소재로 활용이 가능한 유청단백질의 산업화와 관련된 사항들을 조사하고자 수행하였다. 한외여과를 이용한 WPC 제조과정에서 WPC-30을 포함한 한외여과 기의 국산화 가능성을 확인했다. 한외여과, 분무건조 및 단백질분해 효소를 이용하여 제조한 WPC-30 가수분해물의 이화학적 기능성을 검토한 결과 단백질 가수분해능 및 관능성에 대한 평가는 alcalase 처리했을 때 가장 높은 것으로 나타났으며 거품 형성능은 flavourzyme 처리한 WPC-30 가수분해물에서 가장 높은 결과를 보였다. 또한 다양한 pH조건에서의 단백질의 용해도를 측정한 결과, protamex 처리한 WPC-30 가수분해물에서 가장 높은 용해도를 나타내었다. 그러나 모든 WPC-30 가수분해물의 용해도는 알차리 조건에서는 유의적으로 개선되는 효과를 보였다. 이들 결과들을 총체적으로 검토한 결과, 효소를 이용한 유청단백질의 가수분해는 알카리조건에서 alcalase를 사용하는 것이 가장 효과적인 것으로 나타났다.

• Asian-Australasian Journal of Animal Sciences
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• 제32권5호
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• pp.701-710
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• 2019

Objective: This study investigated the effect of different acute heat stress (HS) levels on chicken meat quality and ultra-structure. Methods: Chickens were randomly divided into 7 groups to receive different HS treatments: i) $36^{\circ}C$ for 1 h, ii) $36^{\circ}C$ for 2 h, iii) $38^{\circ}C$ for 1 h, iv) $38^{\circ}C$ for 2 h, v) $40^{\circ}C$ for 1 h, vi) $40^{\circ}C$ for 2 h, and vii) un-stressed control group ($25^{\circ}C$). Blood cortisol level, breasts initial temperature, color, pH, water holding capacity (WHC), protein solubility and ultra-structure were analyzed. Results: HS temperatures had significant effects on breast meat temperature, lightness ($L^*$), redness ($a^*$), cooking loss and protein solubility (p<0.05). The HS at $36^{\circ}C$ increased $L^*{_{24h}}$ value (p<0.01) and increased the cooking loss (p<0.05), but decreased $a^*{_{24h}}$ value (p<0.05). However, as the temperature increased to $38^{\circ}C$ and $40^{\circ}C$, all the values of $L^*{_{24h}}$, cooking loss and protein denaturation level decreased, and the differences disappeared compared to control group (p>0.05). Only the ultimate $pH_{24h}$ at $40^{\circ}C$ decreased compared to the control group (p<0.01). The pH in $36^{\circ}C$ group declined greater than other heat-stressed group in the first hour postmortem, which contributed breast muscle protein degeneration combining with high body temperature, and these variations reflected on poor meat quality parameters. The muscle fiber integrity level in group $40^{\circ}C$ was much better than those in $36^{\circ}C$ with the denatured position mainly focused on the interval of muscle fibers which probably contributes WHC and light reflection. Conclusion: HS at higher temperature (above $38^{\circ}C$) before slaughter did not always lead to more pale and lower WHC breast meat. Breast meat quality parameters had a regression trend as HS temperature raised from $36^{\circ}C$. The interval of muscle fibers at 24 h postmortem and greater pH decline rate with high body temperature in early postmortem period could be a reasonable explanation for the variation of meat quality parameters.

• Journal of Periodontal and Implant Science
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• 제37권1호
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• pp.35-44
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• 2007

Periodontal ligament (PDL) is the connective tissue located between the tooth root and alveolar bone. In a previous study, PDLs22 was isolated as a PDL-specific gene by using subtractive hybrid-ization between cultured PDL fibroblasts and gingival fibroblasts. It was also suggested that PDLs22 plays important roles in the development, differentiation and maintenance of periodontal tissues. However, little is known about functional study of PDLs22 using recombinant protein in PDL fibroblast differentiation and periodontium formation. In this study, in order to produce the PDLs22 recombinat protein, PDLs22 expression vector were constructed and expressed its protein in various host cell and temperature conditions. The results were as follows: 1. PDLs22 protein was not strongly expressed In the induction system using pRSET-PDLs22 construct. 2. When the BL21(DE3) pLysS was used as a expression host, PDLS22 protein was strongly ex-pressed in the induction system using pHCEIIBNd-PDLs22 construct. 3. The PDLs22 protein was recognized at a molecular weight of 28 kDa in western blots. 4. Almost of the expressed PDLs22 protein was not soluble and observed like as inclusion body. 5. The protein solubility was not improved after modification of induction time and temperature during PDLs22 protein production. In this study, the system for the PDLs22 protein production was connstructed. However, the re-results suggest that further studies will be needed to produce the considerable amount of PDLs22 re-combinat protein, which can use for the periodontal regeneration.

• 한국축산식품학회지
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• 제20권4호
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• pp.320-325
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• 2000

The diet had an effect(P<0.05) on the nutritional contents of ostrich meat during 4 month of frozen storage. As frozen storage increased up to 4 months, pJ, water holding capacity(WHC) and myofibrillar protein solu-bility($\mu$g/$\mu$l) were reduced (P<0.05), how-ever, increased drip loss(DL, %) was found in ostrich muscle from forage fed ostriches, This study suggests that forage fed ostriches, This study suggests that frozedn storage(-2$0^{\circ}C$)up to 4 months in ostrich FCL muscle (outside strip)could be reduced protein functionality, due to increase in DL. decrease in WHC, and markedly decrease in myofibrillar protein solubility($\mu$g/$\mu$l).

• 동아시아식생활학회지
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• 제10권5호
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• pp.394-403
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• 2000

The functional properties of sesame protein concentrate(SPC) using different size of ultrafiltration(UF) membranes were examined and compared with those of conventional acid-precipitated sesame protein concentrate. The protein contents of SPC by UF with molecular size of 10K, 30K and look dalton membranes were 84.2%, 82.7%, and 76.4%, respectively, and that of acid-precipitated SPC was 88.7%. The nitrogen solubility of SPC by UF was higher than that of conventional SPC at various pH levels. Especially, it showed three-fold increase at near isoelectric point. However, water absorption capacity and fat absorption capacity of SPC by UF were decreased. For emulsion and foam properties, there were no significant differences between SPC by acid precipitation and SPC by UF method. At various pH levels, SPC by membrane with pore size of 30K dalton showed the highest emulsion properties. The SPC by UF had slightly higher viscosity than defatted sesame flour and SPC by acid precipitation.

• Archives of Pharmacal Research
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• 제25권5호
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• pp.572-584
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• 2002

Rapid development in molecular biology and recent advancement in recombinant technology increase identification and commercialization of potential protein drugs. Traditional forms of administrations for the peptide and protein drugs often rely on their parenteral injection, since the bioavailability of these therapeutic agents is poor when administered nonparenterally. Tremendous efforts by numerous investigators in the world have been put to improve protein formulations and as a result, a few successful formulations have been developed including sustained-release human growth hormone. For a promising protein delivery technology, efficacy and safety are the first requirement to meet. However, these systems still require periodic injection and increase the incidence of patient compliance. The development of an oral dosage form that improves the absorption of peptide and especially protein drugs is the most desirable formulation but one of the greatest challenges in the pharmaceutical field. The major barriers to developing oral formulations for peptides and proteins are metabolic enzymes and impermeable mucosal tissues in the intestine. Furthermore, chemical and conformational instability of protein drugs is not a small issue in protein pharmaceuticals. Conventional pharmaceutical approaches to address these barriers, which have been successful with traditional organic drug molecules, have not been effective for peptide and protein formulations. It is likely that effective oral formulations for peptides and proteins will remain highly compound specific. A number of innovative oral drug delivery approaches have been recently developed, including the drug entrapment within small vesicles or their passage through the intestinal paracellular pathway. This review provides a summary of the novel approaches currently in progress in the protein oral delivery followed by factors affecting protein oral absorption.

• 한국식품과학회지
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• 제38권4호
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• pp.488-494
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• 2006

두부 순물을 UF막으로 농축시켜 제조한 UF 분리농축분말의 일반성분 및 이들 분말을 식품에 첨가할 경우 반드시 고려해야 할 용해도, 유화력, 거품형성능에 대해 살펴보았다. 그 결과 일반 성분에 있어서, UF 분리농축분말의 수분함량과 탄수화물 함량은 순물과 큰 차이가 없었으며 단백질 함량은 순물분말보다 2배가량 높았으나 회분함량은 2배 낮았다. 유지흡착력을 비교 시 ISP>UF 농축분말>순물 순으로 높게 나타났으며 UF 분리농축 분말의 용해도가 ISP와 순물에 비해 높기 때문에 수분흡착력은 매우 미약하였다 UF 분리농축분말의 단백질의 용해도는 등전점 부근인 pH 4.0에서 가장 낮았으며 산성 또는 알칼리성으로 갈수록 증가하는 전형적인 단백질 용해도 곡선을 나타내었다. 유화력은 ISP와는 달리 pH에 따른 현화를 보이지 않으며 150-200 정도의 EAI 값을 나타내었고, 유화안전성은 pH 6.0 이하의 산성에서 더 높은 값을 나타내며 대체로 75-92%의 높은 유화안정성을 보였다. UF 분리농축분말의 거품형성능은 증류수 처리구간에서 ISP와는 달리 pH 4.0-6.0에서 가장 우수하였으며 NaCl 농도가 높을수록 약간 감소하는 경향을 나타내었고, 거품안정성을 측정한 결과 ISP에 비해 대두 단백질의 등전점인 pH 4.0 부근에서 5-7배 높은 거품안정성을 나타내었으나 pH 4.0을 제외한 모든 pH 구간에서 20분 안에 거품이 소멸되었다 UF 분리농축분말은 isoflavone 등 여러가지 기능적 성분을 함유하는 것으로 알려져 있을 뿐만 아니라 용해도, 유화력, 유화안정성, 거품형성능 등이 ISP보다 우수하여 식품가공에서 다양하게 활용될 수 있을 것으로 기대된다.

• 한국수산과학회지
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• 제31권6호
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• pp.823-828
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• 1998

명태 actomyosin 용액에 대한 옥수수전분 가수분해물의 동결 보호 효과는 전기영동상 패턴, 용해도 및 $Ca^{2+}$-ATPase 활성 변화로 알아보았다. 먼저 전기영동상 패턴에서 0일차와 저장 30일차를 비교하였을 때, control의 경우 저장온도에 관계없이 각 band들의 변화가 수반되었고, 특히 MHC의 변화가 두드러졌다. Sucrose 첨가구의 경우, 저장온도에 상관없이 band상의 변화가 거의 없는 것으로 나타났다. 전분가수분해물이 첨가된 시료들에서는 온도 의존성이 현저하여 $-5^{\circ}C$에서 저장한 시료들은 MHC band가 나타나지 않았고 반면에 $-20^{\circ}C$에서는 저장 30일 째에도 0일차와 거의 같은 양상을 보였다. 시료들을 $-5^{\circ}C$에서 저장할 때 용해도 변화는 sucrose의 경우 저장 30일 후에도 $90\%$ 이상의 높은 값을 유지한 반면에 나머지 시료들은 저장과 함께 급속히 감소하였다 $-20^{\circ}C$에서는 sucrose, D.E. 10, 15 및 20을 함유한 시료들은 약 $90\%$ 정도를 나타내었다. 잔존 활성 변화에서도 용해도 변화와 거의 유사한 경향을 나타내었다. 이상에서 살펴보았듯이 명태 actomyosin 용액의 동결변성에 대한 옥수수전분가수분해물들의 보호효과는 저장온도에 따라 많은 차이를 나타내었고, 특히 D.E. 10의 경우는 기존의 동결변성 방지제인 sucrose와 비교하여 $-12^{\circ}C$ 이하에서는 거의 같은 효과를 나타내는 것을 알았고, 저감미, 저열량의 동결변성 방지제로서 가능한 것으로 사료된다.

• Journal of Microbiology and Biotechnology
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• 제30권1호
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• pp.109-117
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• 2020

Cre recombinase is widely used to manipulate DNA sequences for both in vitro and in vivo research. Attachment of a trans-activator of transcription (TAT) sequence to Cre allows TAT-Cre to penetrate the cell membrane, and the addition of a nuclear localization signal (NLS) helps the enzyme to translocate into the nucleus. Since the yield of recombinant TAT-Cre is limited by formation of inclusion bodies, we hypothesized that the positively charged arginine-rich TAT sequence causes the inclusion body formation, whereas its neutralization by the addition of a negatively charged sequence improves solubility of the protein. To prove this, we neutralized the positively charged TAT sequence by proximally attaching a negatively charged poly-glutamate (E12) sequence. We found that the E12 tag improved the solubility and yield of E12-TAT-NLS-Cre (E12-TAT-Cre) compared with those of TAT-NLS-Cre (TAT-Cre) when expressed in E. coli. Furthermore, the growth of cells expressing E12-TAT-Cre was increased compared with that of the cells expressing TAT-Cre. Efficacy of the purified TAT-Cre was confirmed by a recombination test on a floxed plasmid in a cell-free system and 293 FT cells. Taken together, our results suggest that attachment of the E12 sequence to TAT-Cre improves its solubility during expression in E. coli (possibly by neutralizing the ionic-charge effects of the TAT sequence) and consequently increases the yield. This method can be applied to the production of transducible proteins for research and therapeutic purposes.

• 한국식품과학회지
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• 제31권3호
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• pp.586-592
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• 1999

그루, 은파 및 탑동 등의 한국산 소맥분의 단백질 함량은 수입 소맥과 비교하여 상당히 많은 양 함유되어 있으나 탑동을 제외한 한국밀의 반죽 물성은 매우 약하여 단백질의 함량이 많음에도 불구하고 연질맥과 같은 반죽물성을 나타내었고, 특히 그루는 가장 많은 양의 단백질을 함유하지만 전형적인 sticky dough의 문제점을 나타내었다. 수입산과 국내산의 분류에 관계없이 단백질 함량이 많은 그루, 은파, 및 탑동 등의 한국 밀들은 DNS와 같이 acid insoluble protein의 함량이 상대적으로 많으며 water soluble과 salt soluble 단백질의 함량은 상대적으로 적었다. 특히 수입 DNS 밀은 전체 단백질의 함량에 대한 40% 이상이 acid insoluble protein이며 SDS insoluble protein 함량 또한 가장 많은 양 함유되어 있었다. 반면 한국산 소맥은 대부분 연질맥인 WW와 같이 SDS insoluble protein의 함량이 상대적으로 적었다. 또한 품종이나 제품성에 관계없이 밀가루의 단백질 함량이 높을 수록 단백질의 S-S와 SH 함량이 증가하였으며, 이러한 결과는 외국문헌에서 알려진 밀가루의 특성과 특별한 차이가 없었다. 그러나 탑동밀을 제외한 4종의 한국 밀에서 gluten의 특징적인 116 kD 이상의 high molecular weight protein subunit이 관찰되었으며, 이러한 subunit은 high molecular weight glutenin subunit에 해당되는 것으로 외국문헌의 경우 subunit 2.2로 분류하기도 한다. 또한 116 kD영역에 나타나는 triplet band는 탑동을 제외한 4 종의 우리밀은 doublet로 나타나므로 단백질의 high molecular weight subunit region에서 경질맥인 탑동밀의 구조가 가장 수입밀과 일치하는 것을 관찰할 수 있었다.