• Fisheries and Aquatic Sciences
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• 제25권7호
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• pp.357-379
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• 2022

Increased fisheries products have raised by-products that are discarded due to low economic value. In addition, marine by-products are still rich in protein and nutritional value that have biological activities and give benefits to human health. Meanwhile, there is raised pressure for sustainability practices in marine industries to reduce waste and minimize the detrimental effect on the environment. Thus, valorization by-products through bioactive peptide mining are crucial. This review focus on various ways to obtain bioactive peptides from marine by-products through protein hydrolysis, for instance chemical hydrolysis (acid and based), biochemical hydrolysis (autolysis and enzymatic hydrolysis), microbial fermentation, and subcritical water hydrolysis. Nevertheless, these processes have benefits and drawbacks which need to be considered. This review also addresses various biological activities that are favorable in pharmaceutical industries, including antioxidant, antihypertensive, anticancer, anti-obesity, and other beneficial bioactivities. In addition, some potential marine resources of Indonesia for the marine biopeptide from their by-product or undesired marine commodities would be addressed as well.

• 한국식품영양과학회지
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• 제31권1호
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• pp.1-6
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• 2002

강낭콩을 가열한 후 B. subtilis ATCC 51189로 발효시켜 새로운 활성 단백질의 생성여부를 확인하였다. 생강낭콩의 수용성 단백질은 열처리에 의하여 감소하였으며, 발효과정에서 단백질의 양은 변화하지 않았으나, 새로운 아미노산이 합성되었다. 생강낭콩의 수용성 단백질(raw protein, RP)은 분자량 118 kDa의 PHA(phytohemagglutinin)의 전형적인 모습을 보였으나, 열처리한 단백질(heated protein, HP)의 경우, RP의 band는 사라지고, 저분자 peptide로 변화되었으며, 발효과정에 의하여 분자량 18.0 kDa의 새로운 단백질(fermented protein, FP)이 생성된 것을 확인하였다. 또한, RP는 128 HU, HP는 4HU, FP는 32HU의 적혈구응집효과를 보였으며, 위암세포(SNU-1)에 대하여 RP 및 FP는 비교적 높은 농도($IC_{50}$/ $\mu\textrm{g}$/mL)에서 항암활성을 보였다. 그리고, RP 및 FP의 경우 1 $\mu\textrm{g}$/mL에서 림프구 증식효과를 보였고, IFN-${\gamma}$, IL-12의 분비를 촉진하였다. 그러나 HP는 항암효과, 림프구 증식효과, cytokine의 분비촉진효과를 보이지 않았다. 따라서, 강낭콩 lectin은 가열에 의하여 활성물질이 파괴되나, B. subtilis에 의한 발효과정에서 새로운 cytokine 분비촉진물질이 생성되는 것을 확인할 수 있었다.

• Journal of Microbiology and Biotechnology
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• 제28권12호
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• pp.2079-2094
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• 2018

Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the Escherichia coli OmpA and Pseudomonas aeruginosa ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with E. coli YebF, which radiated more than a centimeter from an individual colony of E. coli using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bonded SFTI free in the culture supernatant. To assess the potential of the secreted SFTI to protect the ability of a cytotoxic protein to kill tumor cells, we utilized a tumor-selective form of the Pseudomonas ToxA (OTG-PE38K) alone and expressed as a polycistronic construct with YebF-SFTI in the tumor-targeted Salmonella VNP20009. When we assessed the ability of toxin-containing culture supernatants to kill MDA-MB-468 breast cancer cells, the untreated OTG-PE38K was able to eliminate all detectable tumor cells, while pretreatment with trypsin resulted in the complete loss of anticancer cytotoxicity. However, when OTG-PE38K was co-expressed with YebF-SFTI, cytotoxicity was completely retained in the presence of trypsin. These data demonstrate SFTI chimeras are secreted in a functional form and that co-expression of protease inhibitors with therapeutic proteins by tumor-targeted bacteria has the potential to enhance the activity of therapeutic proteins by suppressing their degradation within a proteolytic environment.

• Asian Pacific Journal of Cancer Prevention
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• 제15권17호
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• pp.7363-7369
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• 2014

The present study aimed to prepare and evaluate polymeric micelles conjugated with folic acid through ${\alpha}$- or ${\gamma}$-carboxyl groups for antitumor efficacy. The isomeric block copolymers, ${\alpha}$- and ${\gamma}$-folate-polyethyleneglycol-distearoyl phosphatidylethanolamine (${\alpha}$- and ${\gamma}$-Fol-PEG-DSPE), were produced by solid phase peptide synthesis. Three types of doxorubicin (DOX)-loaded polymeric micelles (MPEG-DSPE-DOX and ${\alpha}$- / ${\gamma}$-Fol-PEG-DSPEDOX micelles) were prepared via the film formation method. Compared with MPEG-DSPE-DOX micelles, the ${\alpha}$- / ${\gamma}$-Fol-PEG-DSPE-DOX micelles presented a higher cellular uptake behavior in the live cell study. Cell viability percentages were 81.8%, 57.3%, 56.6% at 2 hours for MPEG-DSPE-DOX, ${\alpha}$- and ${\gamma}$-Fol-PEG-DSPE-DOX micelles, respectively (p<0.05). Using the KB xenograft tumor model, both ${\alpha}$- and ${\gamma}$-folate-conjugated micelles were found to have better antitumor effects with lower toxicity in comparison with MPEG-DSPE-DOX micelles. No difference in in vivo antitumor efficacy was found between ${\alpha}$- and ${\gamma}$-Fol-PEG-DSPE-DOX micelles. The folate-conjugated micelles might be a potentially useful strategy for tumor targeting of therapeutic agents, whether grafting with folic acid through ${\alpha}$- or ${\gamma}$-carboxyl groups.