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Choi, Yun Jaie,Lee, Dong Hee,Kang, Seung Ha 생화학분자생물학회 2002 BMB Reports Vol.34 No.2
A time-dependent folding process was used to determine whether or not protein disulfide isomerase (PDI) plays an important role in the maturation of nascent lactoferrin polypeptides. Interaction between lactoferrin and PDI was analyzed according to the co-immunoprecipitation of the two proteins. The results indicate that lactoferrin folding requires a significant interaction with PDI and its binding is relatively brief compared to other nascent polypeptides. The amount of lactoferrin interacting with PDI increases up to half a minute and sharply decreases beyond this time point. During the refolding process that follows reduction by DTT, lactoferrin polypeptides heavily interact with PDI and the interaction period was extended compared to the normal folding process. In terms of the temperature effect on PDI-lactoferrin interaction, PDI binds to lactoferrin polypeptides longer at a lower temperature (here, 25℃) than 37℃. The lactoferrin-PDI interaction was also studied in vitro. According to the in vitro experiment data, PDI was still functional in cell lysates assisting lactoferrin folding into the mature form. PDI interacts with lactoferrin polypeptides for an extended period during the folding in vitro. During the refolding process in vitro, intermolecular aggregates and refolding oligomers matured into a functional form after PDI binds to the lactoferrin. These results suggest that PDI provides a prolonged chaperoning activity in the refolding processes and that there appears to be a greater requirement for PDI chaperone activity in the refolding of lactoferrin polypeptides.
Review : Microencapsulation of Live Probiotic Bacteria
( Chong Su Cho ),( Yun Jaie Choi ),( Cheol Heui Yun ),( Islam Mohammad Ariful ) 한국미생물 · 생명공학회 2010 Journal of microbiology and biotechnology Vol.20 No.10
Scientific research regarding the use of live bacterial cells for therapeutic purposes has been rapidly growing over the years and has generated considerable interest to scientists and health professionals. Probiotics are defined as essential live microorganisms that, when administered in adequate amounts, confer a health benefit on the host. Owing to their considerable beneficial health effects, these microorganisms are increasingly incorporated into dairy products; however, many reports have demonstrated their poor survival and stability. Their survival in the gastrointestinal tract is also questionable. To overcome these problems, microencapsulation techniques are currently receiving considerable attention. This review describes the importance of live probiotic bacterial microencapsulation using an alginate microparticulate system and presents the potentiality of various coating polymers such as chitosan and polylysine for improving the stability of this microencapsulation.
Park, In-Kyung,Lee, Jae-Koo,Cho, Jaie-Soon Asian Australasian Association of Animal Productio 2012 Animal Bioscience Vol.25 No.10
A bacterial isolate derived from soil samples near a cattle farm was found to display extracellular phytase activity. Based on 16S rRNA sequence analysis, the strain was named Bacillus sp. T4. The optimum temperature for the phytase activity toward magnesium phytate (Mg-$InsP_6$) was $40^{\circ}C$ without 5 mM $Ca^{2+}$ and $50^{\circ}C$ with 5 mM $Ca^{2+}$. T4 phytase had a characteristic bi-hump two pH optima of 6.0 to 6.5 and 7.4 for Mg-$InsP_6$. The enzyme showed higher specificity for Mg-$InsP_6$ than sodium phytate (Na-$InsP_6$). Its activity was fairly inhibited by EDTA, $Cu^{2+}$, $Mn^{2+}$, $Co^{2+}$, $Ba^{2+}$ and $Zn^{2+}$. T4 phytase may have great potential for use as an eco-friendly feed additive to enhance the nutritive quality of phytate and reduce phosphorus pollution.
Min, Hae Ki,Choi, Yun Jaie,Cho, Kwang Keun,Ha, Jong Kyu,Woo, Jung Hee 한국미생물 · 생명공학회 1994 Journal of microbiology and biotechnology Vol.4 No.2
The β-1,4-endoglucanase gene from Actinomyces sp. 40 was cloned into Escherichia coli DH5α with pUC19. Chromosomal DNA from Actinomyces sp. 40 was cleaved with the restriction enzyme Sau3Al and ligated into pUC19 for the transformation of Escherichia coli DH5α. Positive clones of β-1,4-endoglucanase gene were detected as the clear zones on a medium supplemented with carboxymethylcellulose (CMC). This transformant possessed a single plasmid, designated pDS1, which contained the vector DNA and a 3.5 kilobase (kb) Sau3Al insertion fragment encoding endoglucanase. The size of the cloned fragment was reduced to 2.0 kb. The endoglucanase activity produced by the E. coli DH5a (pDS6) was higher than that of Actinomyces sp. 40 strain. The optimum pH and temperature of the cloned enzyme were pH 4.0∼5.0 and 55℃, respectively. The cloned enzyme was stable at 55℃ or below and in buffer ranging from pH 4.0 to 7.0. The enzyme degraded CMC but did not degrade xylan, cellobiose, and methyl-umbelliferylcellobiopyranoside (MUC).
Feature Article : Protein and Gene Delivery in Tissue Engineering
( In Yong Kim ),( Jong Hoon Chung ),( Yun Jaie Choi ),( Chong Su Cho ) 한국조직공학과 재생의학회 2008 조직공학과 재생의학 Vol.5 No.4
In regenerative medicine, growing demand for tissues and organs has led to the rapid development of tissue engineering as an alternative. To improve functional scaffold, many biomaterials serve dual purposes; in addition to providing cell support, cutting-edge scaffolds biologically interact with adhering and invading cells and effectively guide cellular growth and development by releasing bioactive proteins and genes. For achieving the ambitious goal of tissue regeneration and replacement, it is more important to understand the basic principles of protein and gene delivery as well as design of the system required by using proper biomaterials. This review covered the requirement in the materials choice, the strategies, the main techniques for producing proteins and genes releasing scaffolds.