• Journal of the Korean Wood Science and Technology
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• 제38권2호
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• pp.140-148
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• 2010

This study was to investigate the enzymatic hydrolysis of cellulose using the cellulase from whole body of the native termite collected in Milyang-si, Kyungsangnamdo, Korea. In the results, optimal temperature and pH for the enzyme of native termites were $45^{\circ}C$ and pH 5.5 for both endo-${\beta}$-1, 4-glucanase and ${\beta}$-glucosidase. Enzyme activity of the termite enzyme was shown $8.8{\times}10^{-2}\;FPU/m{\ell}$. And the highest glucose hydrolysis rate of cellulose by the digestive enzyme from test termites was 24.5% based on the glucan, comparing 59.7% by commercial enzyme (only celluclast 1.5 L) at 1% (w/v) substrate and 36 hours in hydrolysis time. This hydrolysis rate by the digestive enzyme from test termites was comparatively high value in 41% level of the commercial enzyme. When cellulose was hydrolyzed by the digestive enzyme of the native termite, glucose hydrolysis was almost completed in 12 hours which was the considerably reduced time for cellulose hydrolysis. It was suggested that the quiet short reaction time for cellulose hydrolysis by the enzyme from native termite could be a very high advantage for development of hydrolysis cellulase for lignocellulosic biomass.

• Journal of Microbiology and Biotechnology
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• 제24권2호
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• pp.245-253
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• 2014

A fibrinolytic enzyme was produced by an edible mushroom of Pleurotus ostreatus using submerged culture fermentation. The enzyme was purified from the culture supernatant by applying a combination of freeze-thaw treatment, ammonium sulfate precipitation, hydrophobic interaction, and gel filtration chromatographies. The enzyme was purified by a 147-fold, with a yield of 7.54%. The molecular masses of the enzyme an determined by gel filtration and SDS-PAGE were 13.6 and 18.2 kDa, respectively. The isoelectric point of the enzyme was 8.52. It hydrolyzed fibrinogen by cleaving the ${\alpha}$ and ${\beta}$ chains of fibrinogen followed by the ${\gamma}$ chains, and also activated plasminogen into plasmin. The enzyme was optimally active at $45^{\circ}C$ and pH 7.4. The enzyme activity was completely inhibited by EDTA, whereas protease inhibitors of TPCK, SBTI, PMSF, aprotinin and pepstatin showed no inhibition on its activity. The partial amino acid sequences of the enzyme as determined by Q-TOF2 were ATFVGCSATR, GGTLIHESSHFTR, and YTTWFGTFVTSR. These sequences showed a high degree of homology with those of metallo-endopeptidases from P. ostreatus and Armillaria mellea. The purified enzyme can also be applied as a natural agent for oral fibrinolytic therapy or prevention of thrombosis.

• Asian-Australasian Journal of Animal Sciences
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• 제16권9호
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• pp.1369-1373
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• 2003

ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

• Journal of Animal Science and Technology
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• 제51권1호
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• pp.39-44
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• 2009

본 연구는 목재부후균 유래 $\beta$-글루코시다제, 엑소글루카나제 및 엔도글루카나제 유전자를 함유한 형질전환체 효모를 배양한 액상섬유소분해효소에 대하여 인공반추위 배양시험을 통해 완전혼합사료에 대한 적용 수준 조사와 더불어 한우 비육 거세우의 사양시험을 통해 2 종류의 액상섬유소분해효소를 완전혼합사료에 1.0% 수준으로 첨가 급여하여 가축의 성장, 영양소소화율에 미치는 영향을 알아보고자 실시하였다. 1. 인공반추위 배양시험을 통해 완전혼합사료에 대한 액상 섬유소분해효소 첨가에 의해 pH가 약간 증가하는 경향이었다. 휘발성지방산에서 acetate 비율이 배양 12와 24시간에 유의적으로(p<0.05) 높게 나타났으며 총휘발성지방산 농도 역시 배양 12와 24시간에 유의적으로(p<0.05) 증가시켰으며 1.0% 첨가구에서 효과적이었다. 건물소화율은 배양 24시간에 액상 섬유소분해효소 첨가구에서 유의적으로(p<0.05) 증가하였다. 2. 한우 거세우 사양시험에서는 액상 섬유소분해효소 급여에 의해 일당증체량과 사료효율이 개선되는 경향이었다. 영양소 소화율에서는 DM, 조섬유, NDF 및 ADF 소화율이 액상 섬유소분해효소 첨가에 의해 유의적으로(p<0.05) 증가하였다. 따라서 인공반추위 배양시험을 통해 액상 섬유소분해효소 1.0% 첨가가 비교적 반추위발효 양상을 개선시키었으며, 한우 사양시험에서도 2종류의 액상 섬유소분해효소 1.0% 급여가 일당증체량 및 사료효율 개선효과가 있었다.

• Journal of Microbiology and Biotechnology
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• 제20권2호
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• pp.332-339
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• 2010

The lipase from Mucor racemosus NRRL 3631 was partially purified by fractional precipitation using 60% ammonium sulfate, which resulted in a 8.33-fold purification. The partially purified lipase was then immobilized using different immobilization techniques: physical adsorption, ionic binding, and entrapment. Entrapment in a 4% agar proved to be the most suitable technique (82% yield), as the immobilized lipase was more stable at acidic and alkaline pHs than the free enzyme, plus 100% of the original activity was retained owing to the thermal stability of the immobilized enzyme after heat treatment for 60 min at $45^{\circ}C$. The calculated half-lives (472.5, 433.12, and 268.5 min at 50, 55, and $60^{\circ}C$, respectively) and the activation energy (9.85 kcal/mol) for the immobilized enzyme were higher than those for the free enzyme. Under the selected conditions, the immobilized enzyme had a higher $K_m$ (11.11 mM) and lower $V_{max}$ (105.26 U/mg protein) when compared with the free enzyme (8.33 mM and 125.0 U/mg protein, respectively). The operational stability of the biocatalyst was tested for both the hydrolysis of triglycerides and esterification of fatty acids with glycerol. After 4 cycles, the immobilized lipase retained approximately 50% and 80% of its original activity in the hydrolysis and esterification reactions, respectively.

• 대한화장품학회지
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• 제26권1호
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• pp.81-92
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• 2000

Development of stabilized enzyme was attempted for cosmetic applications. Papain, a proteolytic enzyme, was stabilized through conjugation with a soluble carbohydrate biopolymer, SC-glucan$^{TM}$ . With a novel structure of the conjugation site, stability of the enzyme was significantly enhanced such that more than 90% of the initial activity retained after a month storage at 45$^{\circ}C$, while no activity were detected in native enzyme or enzyme simply mixed with SC-glucan$^{TM}$ after the storage. Conjugation with SC-glucan$^{TM}$ not only extended the half-life of the enzyme on storage at higher temperature, but was also found to protect enzymes against some components contained in cosmetic products for skin care. Cosmetic lotion containing 1 % papain conjugate was more effective and less irritative in exfoliating stratum corneum of human skin than the lotion containing 5% lactic acid, one of the current popular exfoliating agents.gents.

• Journal of the Korean Wood Science and Technology
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• 제38권5호
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• pp.421-428
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• 2010

This study investigated on enzyme production in the digestive organs of the native termite (Reticulitermes speratus) in Milyang, Korea. Four types of major cellulases [EG (endo-1,4-${\beta}$-glucanase), BGL (${\beta}$-glucosidase), CBH (cellobiohydrolase) and BXL (${\beta}$-1,4-xylosidase)] were present in the digestive organs of the termite. The strong enzyme activity for BGL was found from the native termite, and also shown that the enzyme was distributed in the salivary gland, foregut, and hindgut. BXL, which breaks down hemicellulose near the amorphous region, was detected mainly from salivary gland, foregut, and midgut. However, CBH was distributed mainly in the hindgut. Meanwhile, EG which degrades cellulose, was found mainly in the hindgut and salivary glands. These facts indicate that celluases production patterns are differ from different sites compare to the same species found in Japan, suggesting that enzyme production in the digestive organs of termites is changed according to their habitats.

• 생약학회지
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• 제19권1호
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• pp.19-27
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• 1988

The hexane and ether extracts from the roots of Angelica dahurica caused a significant inhibition of hepatic drug-metabolizing enzyme (DME) activity. Through systematic fractionation by $SiO_2\;column$ and vacuum liquid chromatography monitoring by bioassays, three furanocoumarins, phellopterin, byakangelicin and tert-O-methylbyakangelicin were isolated as active principles. These components have biphasic responses, both inhibitory and inducing effects on DME system. Tert-O-methyl byakangelicin was found to have the strongest enzyme inhibitory potency.

• 한국축산식품학회지
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• 제34권6호
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• pp.742-748
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• 2014

This study was conducted to evaluate the activities of antioxidant enzyme (glutathione peroxidase (GSH-Px)) and lysosomal enzymes (alpha-glucopyranosidase (AGP) and beta-N-acetyl-glucosaminidase (BNAG)) of the longissimus dorsi (LD) muscle from Hanwoo (Korean cattle) in three freezing conditions. Following freezing at -20, -60, and $-196^{\circ}C$ (liquid nitrogen), LD samples (48 h post-slaughter) were treated as follows: 1) freezing for 14 d, 2) 1 to 4 freeze-thaw cycles (2 d of freezing in each cycle), and 3) refrigeration ($4^{\circ}C$) for 7 d after 7 d of freezing. The control was the fresh (non-frozen) LD. Freezing treatment at all temperatures significantly (p<0.05) increased the activities of GSH-Px, AGP, and BNAG. The $-196^{\circ}C$ freezing had similar effects to the $-20^{\circ}C$ and $-60^{\circ}C$ freezing. Higher (p<0.05) enzymes activities were sustained in frozen LD even after 4 freeze-thaw cycles and even for 7 d of refrigeration after freezing. These findings suggest that freezing has remarkable effects on the activities of antioxidant enzyme and lysosomal enzymes of Hanwoo beef in any condition.

• Journal of Microbiology and Biotechnology
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• 제32권6호
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• pp.749-760
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• 2022

α-Galactosidase is a debranching enzyme widely used in the food, feed, paper, and pharmaceuticals industries and plays an important role in hemicellulose degradation. Here, T26, an aerobic bacterial strain with thermostable α-galactosidase activity, was isolated from laboratory-preserved lignocellulolytic microbial consortium TMC7, and identified as Parageobacillus thermoglucosidasius. The α-galactosidase, called T26GAL and derived from the T26 culture supernatant, exhibited a maximum enzyme activity of 0.4976 IU/ml when cultured at 60℃ and 180 rpm for 2 days. Bioinformatics analysis revealed that the α-galactosidase T26GAL belongs to the GH36 family. Subsequently, the pET-26 vector was used for the heterologous expression of the T26 α-galactosidase gene in Escherichia coli BL21 (DE3). The optimum pH for α-galactosidase T26GAL was determined to be 8.0, while the optimum temperature was 60℃. In addition, T26GAL demonstrated a remarkable thermostability with more than 93% enzyme activity, even at a high temperature of 90℃. Furthermore, Ca²⁺ and Mg²⁺ promoted the activity of T26GAL while Zn²⁺ and Cu²⁺ inhibited it. The substrate specificity studies revealed that T26GAL efficiently degraded raffinose, stachyose, and guar gum, but not locust bean gum. This study thus facilitated the discovery of an effective heat-resistant α-galactosidase with potent industrial application. Meanwhile, as part of our research on lignocellulose degradation by a microbial consortium, the present work provides an important basis for encouraging further investigation into this enzyme complex.