• Proceedings of the Korean Society of Crop Science Conference
• /
• 2006.04a
• /
• pp.644-645
• /
• 2006

• Proceedings of the Korean Society of Sericultural Science Conference
• /
• 2002.10a
• /
• pp.78-78
• /
• 2002

No Abstract, See Full Text

• Korean Journal of Pharmacognosy
• /
• v.35 no.3 s.138
• /
• pp.233-238
• /
• 2004

Lipoprotein-associated phospholipase $A_2\;(Lp-PLA_2)$ is a potential biomarker of coronary heart disease and plays an important proinflammatory role in the progression of atherosclerosis. Also acyl-CoA: cholesterol acyltransferase (ACAT) and oxidized low-density lipoprotein (LDL) playa key role in atherosclerosis, respectively. And so, the inhibitory activities of the methanol extracts of 42 insect resources were examined on $Lp-PLA_2$, ACAT, and LDL oxidation for screening of anti-atherogenic substances. Among them, the methanol extracts of Eurydema rugosa significantly inhibited all of upper three activities. Several kinds of tested insects having high inhibitory effect with the methanol extracts were extracted with n-hexane, ethyl acetate, and acetone, and their inhibitory activities were tested.

• Korean Journal of Agricultural Science
• /
• v.45 no.4
• /
• pp.655-663
• /
• 2018

The insect gut microbiome is known to have important roles in host growth, development, digestion, and resistance against pathogens. In addition, the genetic diversity of the insect gut microbiota has recently been recognized as potential genetic resources for industrial bioprocessing. However, there is limited information regarding the insect gut microbiota to better help us understand their potential benefits for enhanced pig production. With the development of next-generation sequencing methods, whole genome sequence analysis has become possible beyond traditional culture-independent methods. This improvement makes it possible to identify and characterize bacteria that are not cultured and located in various environments including the gastrointestinal tract. Insect intestinal microorganisms are known to have an important role in host growth, digestion, and immunity. These gut microbiota have recently been recognized as potential genetic resources for livestock farming which is using the functions of living organisms to integrate them into animal science. The purpose of this literature review is to emphasize the necessity of research on insect gut microbiota and their applicability to pig production or bioindustry. In conclusion, bacterial metabolism of feed in the gut is often significant for the nutrition intake of animals, and the insect gut microbiome has potential to be used as feed additives for enhanced pig performance. The exploration of the structure and function of the insect gut microbiota needs further investigation for their potential use in the swine industry particularly for the improvement of growth performance and overall health status of pigs.

• Proceedings of the Korean Society of Applied Entomolohy Conference
• /
• 2005.05a
• /
• pp.150-150
• /
• 2005

• Proceedings of the Korean Society of Applied Entomolohy Conference
• /
• 2005.05a
• /
• pp.151-151
• /
• 2005

• 축산식품과학과 산업
• /
• v.7 no.1
• /
• pp.21-23
• /
• 2018

• Proceedings of the Korean Society of Applied Entomolohy Conference
• /
• 2001.11a
• /
• pp.143-143
• /
• 2001

• Proceedings of the Korean Society of Applied Entomolohy Conference
• /
• 2000.10a
• /
• pp.22-22
• /
• 2000

• Journal of Microbiology and Biotechnology
• /
• v.17 no.5
• /
• pp.761-768
• /
• 2007

Serratia proteamaculans HY-3 isolated from the digestive tract of a spider produces an extracellular protease named arazyme, with an estimated molecular mass of 51.5 kDa. The purified enzyme was characterized as having high activities at wide pH and temperature ranges. We further characterized biochemical features of the enzymatic reactions under various reaction conditions. The protease efficiently hydrolyzed a broad range of protein substrates including albumin, keratin, and collagen. The dependence of enzymatic activities on the presence of metal ions such as calcium and zinc indicated that the enzyme is a metalloprotease, together with the previous observation that the proteolytic activity of the enzyme was not inhibited by aspartate, cysteine, or serine protease inhibitors, but strongly inhibited by 1,10-phenanthroline and EDTA. The araA gene encoding the exoprotease was isolated as a 5.6 kb BamHI fragment after PCR amplification using degenerate primers and subsequent Southern hybridization. The nucleotide sequence revealed that the deduced amino acid sequences shared extensive similarity with those of the serralysin family of metalloproteases from other enteric bacteria. A gene(inh) encoding a putative protease inhibitor was also identified immediately adjacent to the araA structural gene.