표고 재배용 액체종균 배지조성은 대두박분 배지에 입도가 850 μm이하인 참나무분 0.3% 첨가 시 균사체 건중량이 457 mg으로 다소 높았으며, Laccase 활성도는 참나무분 첨가율별 대두박분 배지에 큰 차이가 없었으나 Cellulase 활성도는 CMC Agar Plate에서 26.4 mm로서 참나무분 첨가율별 대두박분 액체종균 처리구중에서 가장 우수하였다. 액체종균의 통기량이 증가할수록 이산화탄소 발생량이 증가하여 배양 7일째 최대치를 나타내었으며 균사체 건중량은 10일째 3.0g/l로 가장 우수한 것으로 나타났다. 통기량이 증가할수록 이산화탄소 발생량, 균사체 건중량도 증가하였으며 0.6vvm 처리시 배지 증발율이 32%, 균사체 건중량이 3.5g/l로서 우수하였다. 선발된 액체종균을 톱밥 종균과 생산성 비교를 위하여 톱밥재배 봉지배지에 시험한 결과, 액체종균의 생육기간이 톱밥종균에 비해 1일 지연되었으나, 봉지당 유효 개체수와 수량에는 유의적인 차이가 없는 것으로 나타났다.

Some bioactive peptides have been identified by activity-guided fractionation. However, it is difficult to prepare or synthesize enough amounts of active peptides for food ingredients and for animal or human trials. The objective of the present study was to prepare peptide fractions of sufficient amounts with high antioxidant activity which could be applied to the food and animal model. Oyster hydrolysate was fractionated the basis of the amphoteric nature of sample peptides by preparative isoelectric focusing (autofocusing). To monitor the fractionation of peptides by autofocusing, amino acid analysis of the autofocusing fractions was performed. Each autofocusing fraction was evaluated by 1,1-diphenyl-2-picrylhydrazyl (DPPH) and hydroxyl (OH) radical scavenging activities, oxygen radical absorbance capacity (ORAC), and Fe 2+ chelatingassays. More than 40% of the peptides were distributed between Fr. 4 and 7 (pH<5.0). Approximately 16% of the peptides were recovered in basic fractions (pH>10.0; Fr. 9-10). 11 % of peptides were recovered in the neutral fraction (6.0<pH<7.0; Fr. 8). The peptides in the acidic and basic fractions are characterized by a higher content of acidic and basic amino acids, respectively. Acidic fraction showed higher ORAC values than crude oyster hydrolysate. Also, the acidic fraction showed high DPPH and OH radical scavenging activity. On the other hand, basic fraction showed higher chelating ability than crude oyster hydrolysate. In the present study, oyster peptide fractions of large-scale with high antioxidant activity were successfully fractionated by autofocusing for food additives and animal trials.

Most insects possess two different acetylcholinesterases (AChEs) (i.e., AChE1 and AChE2). It has been recently reported that both AChEs are equally active in a damselfly species, providing a unique example of the incomplete specialization of one AChE function after duplication (Kim and Lee, 2013). In this study, we investigated the tissue distribution patterns and the molecular and inhibitory properties of two AChEs (i.e., VgAChE1 and VgAChE2) from the Vestalis gracilis damselfly. VgAChEs exhibited almost identical catalytic activity and were expressed in the central nervous system (CNS). The most predominant molecular form of both VgAChEs was a disulfide-bridged dimer, which is associated with the cell membrane via a glycosylphosphatidylinositol anchor. In an inhibition assay, however, VgAChE1 and VgAChE2 exhibited different sensitivities to organophosphate and carbamate insecticides depending on the structure of the inhibitors. These findings suggest that both VgAChEs have neuronal functions. In addition, soluble monomeric and cleaved molecular forms were detected in both the CNS and peripheral nervous system tissues by an AChE2-specific antibody, implying that VgAChE2 probably shares both neuronal and non-neuronal physiological functions in V. gracilis. Our results support the notion that both VgAChEs, paralogous of each other, are involved in synaptic transmission, with VgAChE2 being in the early stage of acquiring non-neuronal functions.

This study investigated the effect of kilning condfition on the diastatic power and activities of protease, α-amylase, and β-amylase in rice malt. Common rice (Oryza sativa) was steeped at 30℃ for 50 h, germinated at 30℃ for 7 days, and kilned at 50℃ for 24 h. The moisture content and enzymatic activities were determined under various kilning times. As a result, the moisture content was reduced from 42.1 % to 3.9% after 24 h of kilning at 50℃. The protease activity of rice malt showed lower value than that of barley malt. All enzymatic activities were decreased during the kilning stage. Results indicated that after prolonged kilning at 50℃, the inactivation of hydrolytic enzymes might be occurred. Even though the amylolytic activity of malted rice showed low value, the rice malt shows the potential characteristics as ingredient for the brewing and cereal industries.

무당벌레(Harmonia axyridis)의 중장 내에서 먹이 단백질이 소화되는 과정을 연구하기 위하여 진딧물과 생간의 AP를 모델 단백질로 이용하였다. 천역 먹이인 긴꼬리볼록진딧물(Megoura crassicauda)과 인공먹이인 닭의 생간은 각각 고유의 acid phosphatase(AP)를 가지고 있으며, 무당벌레의 중장 내부로 들어온 후에도 활성을 나타내었다. 무당벌레의 장에서 자체적으로 생성하여 중장 내부로 분비하는 AP는 관찰되지 않았다. 무당벌레의 단백질 소화력은 먹이의 종류에 따라 차이를 나타내는 경향을 보였다. 생간의 AP는 무당벌레 중장내에서 12시간이 지나면 거의 활성을 잃어 버리나 긴꼬리볼록 진딧물의 AP는 24시간이 경과하여도 강한 활성을 나타내었다.

The antioxidative activity of various enzymatic extracts from Sarcodon aspratus (S. aspratus) was evaluated by measuring 1,1-diphenyl-2-picrylhydrazyl (DPPH), and alkyl radical scavenging activity using an electron spin resonance (ESR) spectrometer. For this study, the S. aspratus were enzymatically hydrolyzed by seven carbohydrases (Viscozyme, Celluclast, Dextrozyme, AMG, Promozyme, Maltogenase, and Termamyl) and eight proteases (α-chymotrypsin, Alcalase, Flavourzyme, Neutrase, papain, pepsin, Protamax, and trypsin). The DPPH radical scavenging activities of Viscozyme and pepsin extracts were the highest, and the half maximal inhibitory concentration (IC50) values were 0.896 and 0.734mg/mL, respectively. The Celluclast and trypsin extracts showed the highest scavenging activities on alkyl radical, and their IC50 values were 0.278 and 0.575mg/mL, respectively. The Celluclast extracts was decreased cell apoptosis in PC-12 cells against H2O2-induced oxidative damage. The findings of the present study suggest that enzymatic extracts of S. aspratus exhibit antioxidative activity against oxidative stress on PC-12 cells.

Heavy metals like Mercury and Cadmium cause various kinds of toxicities in the organs of Liver and Kidney. To observe the results of toxicity in the liver, kidney, and serum when the rats were injected subcutaneously with HgCl2 and CdCl2 and sacrificed after 24 hours and 72 hours from the last injection, we measured variation of lipidperoxide values in rat liver homogenate, variation of aspartate aminotransferase and alanine aminotransferase in rat serum. Variation of lipidperoxide values in rat kidney homogenate and variation of BUN in rat serum. It was found that Mercury and Cadmium administered subcutaneously to the skin in the air could cause the damages of liver and kidney.