• International Journal of Industrial Entomology and Biomaterials
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• v.2 no.1
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• pp.7-13
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• 2001

Enzymatic hydrolysis of different forms of silk fibroin (soluble, gel and insoluble forms) by industrial and commercial enzyme preparations to obtain aqueous and powdered silk fibroin in relatively mild conditions was investigated. A mono-enzymatic hydrolysate systems were tested for hydrolysis of water-soluble form of fibroin as most productive form of protein substrate. Insoluble forms of substrate usually were hydrolyzed less effective. In some cases from soluble fibroin substrate gel was formed during hydrolysis process. This hindered intermixing and decreased rates of hydrolysis. Insoluble sediments were formed in enzymatic hydrolysates in other cases. These sediments and also sediment after chemical hydrolysis were purified and tested on amino acids content for comparison. Sediments formation in these conditions are considered as pure tyrosine isolation method. Obtained hydrolysates were characterized by gel-chromatography analysis and other standard biochemical methods. Possibility of application of enzymatic hydrolysis for preparation of silk fibroin hydrolysates is discussed.

• The Korean Journal of Food And Nutrition
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• v.10 no.1
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• pp.87-91
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• 1997

Isomaltooligosaccharides in Sikhye were digested with enzyme (30unit/ml) of $\alpha$-amylase, $\alpha$-glucosidase and glucoamylase from Aspergillus awamori, sweet potato $\beta$-amylase and human salivary $\alpha$-amylase at 37$^{\circ}C$ for 1 hour, respectively. These amylases acted on these saccharides to give hydrolysis products with less than 20% of degree of hydrolysis, except the case of glucoamylase with 62% of high degree of hydrolysis. $\alpha$-Glucosidase plus human salivary $\alpha$-amylase hydrolyzed it to attain the hydrolysis value up to 25%, but further increment of hydrolysis was not observed. Rice residue in Sikhye has similar sugar composition and structure, judging from sugar analyses by the enzymatic hydrolysis. These results suggest that isomaltooligosaccharides and rice residue in Sikhye can be a growth factor for Bifidobacterium and dietary fiber which is useful for human health.

• 한국신재생에너지학회:학술대회논문집
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• 2006.06a
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• pp.485-488
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• 2006

In order to investigate the possibility of waste mushroom logs as biomass resource chemical and physical characteristics of normal woods and waste mushroom logs such as crystallinity value, energy consumption, total sugar yield after hydrolysis chemical compounds and molecular weight distribution after acid hydrolysis, were examined. In the results, crystallinity of waste mushroom logs which were three year passed after the inoculation was decreased drastically from 49% to 33% during the cultivation. Lignin contents as chemical compounds of normal woods and waste mushroom logs were 21.07% and 18.78%, respectively. By the results of measurement of energy consumption, the size reduction of normal woods required a significantly higher energy than that of waste mushroom logs. In the hydrolysis, total sugar yield by enzyme and acid hydrolysis were high in waste mushroom logs(53% 57.5%) than in normal woods(42.9%, 47.17%). According to the molecular weight distribution using GPC, low molecular weight compounds were distributed in waste mushroom logs. Based on these results, waste mushroom logs have enough potential as material for developing alternative energy because of easily conversion to sugar by various hydrolysis methods and requirement of low energy consumption during size reduction.

• 한국신재생에너지학회:학술대회논문집
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• 2010.11a
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• pp.105.2-105.2
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• 2010

전처리 후 얻어진 셀룰로스 고분자를 단당류로 전환하기 위해서는 셀룰라제를 이용한 당화 과정이 필요하다. 통상 실험식 연구에서는 셀룰로스 당화시 당수율을 최대로 하기위해 pH조절을 위한 Citrate buffer와 미생물 오염을 막기 위한 Autoclave에서의 멸균 과정을 거친다. 하지만 대량생산을 목적으로 하는 산업체에서는 적용이 어렵다는 문제점이 있다. 따라서 본 연구에서 이를 대신하여 산업체에서 적용 가능한 당화전환 공정의 효율성을 평가하고자 하였다. Autoclave 멸균을 대체하는 공정으로 항생제 첨가와 여과에 의한 제균을 선택하였고, citrate buffer를 대신하여 buffer를 첨가하지 않은 물을 pH를 조정하여 사용 하였다.실험결과 기존의 당화공정을 사용하였을 때 당화율이 81%이었고, pH를 조절한 제균 water에 항생제를 첨가하는 공정은 71%로 나머지 배지들 중 가장 높은 당화율을 나타냈다. 이것은 기존의 당화율보다 10% 낮은 수치이나 공정비를 교려하여 봤을 때 효율성 있는 공정으로 판단된다.

• Journal of Microbiology and Biotechnology
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• v.4 no.2
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• pp.85-94
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• 1994

Lipase (triacylglycerol hydrolase, EC 3.1.1.3) is able to catalyze the hydrolysis of ester bonds of triacylglycerols at the interface between aqueous phase and organic phase containing substrate. With the rapid development of lipid biotechnology, lipase-catalyzed hydrolysis of lipids has a great concern from the industrial point of view. Owing to the reversible nature of the lipase, the reactions are also applied for glyceride synthesis, interesterification and resolution of racemic mixtures into optically active alcohols or acids. For all applications of the lipases, a reliable method for the determination of enzyme activity is required. Precise quantitative determination of its activity is essential as the basis of research and development of the bioprocess involving the enzyme. This article reviews the existing literature on the detection and determination of lipase activity from microbial, mammalian and plant sources.

• Korean Journal of Pharmacognosy
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• v.7 no.2
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• pp.85-93
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• 1976

Since cellulose is the only organic material that is annually replenishable in very large quantities, we must explore ways to utilize it as a source of energy, food and chemicals. For the utilization of this resource, it is first enzymatic hydrolyzed to glucose, then the glucose can be used as a food, converted single cell protein by microorganism, fermented to clean burning fuel and other chemicals. Cellulolytic enzyme, cellulase, consists of two or three major components, $C_1-cellulase$, $C_x-cellulase$ and ${\beta}-glucosidase$. $C_x-cellulase$ are fairly common but $C_1-cellulase$ are quite rare. Trichoderma viride is the best source of active cellulose, especially $C_1-enzyme$. Saccharification rate of cellulose in greatly influenced by the degree of crystallinity and extent of lignification. But by the pretreatment the substrate with cellulose swelling agent, delignifying reagent and physical treatment, the degree of saccharification is enhanced. Thus, glucose syrups of 2 to 10% concentration are realized from milled newspaper. The enzymatic hydrolysis of such energy rich material, such as cellulose, to glucose is technically feasible and practically achievable on a very large scale.

• Bulletin of the Korean Chemical Society
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• v.4 no.2
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• pp.72-76
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• 1983

Cephaloglycin was synthesized directly from D-${\alpha}$ -phenylglycine methyl ester and 7-aminocephalosporanic acid using whole cell enzyme of Xanthomonas citri (IFO 3835). Some optimal conditions for cephaloglycin synthesis were investigated, and yield improvements for its production by several methods were attempted. Using the whole cell enzyme system, the reaction kinetic model for cephaloglycin synthesis is proposed, and the kinetic constants for D-${\alpha}$ -phenylglycine methyl ester hydrolysis, cephaloglycin synthesis, and cephaloglycin hydrolysis were determined. The $K_m$ values of D-${\alpha}$-phenylglycine methyl ester, 7-aminocephalosporanic acid, and cephaloglycin were 11 mM, 24 mM, and 167 mM, and $K_i$ value of D-${\alpha}$-phenylglycine was 15 mM, respectively. The pattern of product inhibition was found to be competitive one.

• Journal of Microbiology and Biotechnology
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• v.16 no.3
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• pp.408-413
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• 2006

A strain, P821, with phospholipase D activity was isolated from soil and identified as a Streptomyces species. The phospholipase D enzyme was purified from a culture broth of the isolated strain using ammonium sulfate precipitation and DEAE-Sepharose, phenyl-Sepharose, and Superose 12 HR column chromatographies. The purified enzyme exhibited an optimum temperature and pH of $55^{\circ}C$ and 6.0, respectively, in the hydrolysis of phosphatidylcholine and remained stable up to $60^{\circ}C$ within a pH range of 3.5-8.0. The enzyme also catalyzed a transphosphatidylation reaction to produce phosphatidylserine with phosphatidylcholine and serine substrates. The optimum conditions for the transphosphatidylation were $30^{\circ}C$ and pH 5.0, indicating quite different optimum conditions for the hydrolysis and transphosphatidylation reactions. The gene encoding the enzyme was cloned by Southern hybridization and colony hybridization using a DNA probe designed from the conserved regions of other known phospholipase D enzymes. The resulting amino acid sequence was most similar to that of the PLD enzyme from Streptomyces halstedii (89.5%). Therefore, the enzyme was confirmed to be a phospholipase D with potential use in the production of phosphatidylserine.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1979.04a
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• pp.113.2-114
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• 1979

$\beta-Galactosidase$ is an enzyme which catalizes hydrolysis of lactose, a natural substrate, to glucose and galctose and transferring some monosac-charide units to active acceptors as sugar or alcohol. The occurence of $\beta-Galactosidase$ is known in various microorganisms, animals and higher plants and has been studied by many investigatigators. Especially, a great deal of articles for the enzyme of E. coli have been presented in genetic control mechanism and induction-repression effects of proteins, On the other hand, in the dairly products industry, it is important to hydrolyes lactosd which is the principal sugar of milk and milk products. During the last few years, the interest in enzymatic hydrolysis of milk lactose has teen increased, because of the lactose intolerence in large groups of the population. Microbial $\beta-Galactosidases$ are considered potentially most suitable for processing milk to hydrolyse lactose and, in recent years, the immobilized enzyme from yeast has been examined. Howev, most of the microbial $\beta-Gal$ actosidase are intracellular enzymes, except a few fungal $\beta-Gala-$ ctosidases, and extracellular $\beta-Galactosidase$ which may be favorable to industrial applieation is not so well investigated. On this studies, a mold producing a potent extracellular $\beta-Galactosidase$ was isolated from soil and identified as an imperfect fungus, Beauveria bassians. In this strain, both extracellular and intracellular $\beta-Galactosidases$ were produced simultaneously and a great increase of the extracellular production was acheved by improving the cultural conditions. The extracellular enzyme was purified more than 1, 000 times by procedures including Phosphocellulose and Sephadex G-200 chromatographies. Several characteristics of the enzymewas clarified with this preparation. The enzyme has a main subunit of molecular weight of 80, 000 which makes an active aggregate. And at neutral pH range, it has optimum pH for activity and stability. The Km value was determined to be 0.45$\times$10$^{-3}$ M for $o-Nitrophenyl-\beta-Galactoside.$ In any event, it is interesting to sttudy the $\beta-Galactosidase$ of B. bassiana for the mechanism of secretion and conformational structure of enzyme.

• Bulletin of the Korean Chemical Society
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• v.22 no.4
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• pp.427-428
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• 2001