In the experiment of cholesterols and steroidal compounds. gas chromatography has been widely used to determine the compounds. Without the facility, we could determine the amount of 17-ketosteroids in the use of t. 1. c technique. In the muicrobial conversion of cholesterol to 17-ketsoteroids, $\alpha,$ $\alpha'-dipyridyl$ which might be a inhibitor of $9\alpha-hydroxylase$ of steroid skeleton was added to microbial culture broth. The inhibitor contaminated due to its solubility in organic solvents and hindered the determination of 17-ketost eroids on t.1. c in all the process of the experiment. we successfully determined the 17-ketosteroids by the use of Ag$^{+}$ band on t. 1. c. plate.e.

Each year, vast amount of agricultural crop residues are produced (about 60 percent of the total crop production), which have not been effectively utilized because they are bulky and lignocellulosic, thus having little fuel energy per unit volume. Using treated plant residues as animal feeds could result in an ultimate saving of fossil fuel energy and a more effective utilizat ion of products created by the photosynthetic process. Feeding the residues to animals would decrease the pollution potential, but these residues are difficult for even a ruminant animal to digest. If cellulosic wastes produced from cereal grain straw and wood could be digested, land now used for producing forage add grain cnuld be shifted to food crops for humans. During the past decade, considerable efforts were made to utilize crop residues. These utilization methods can be broadly grouped into for categories: (1) direct uses, (2) mechanical conversions, (3) chemical conversions and (4) biological conversions. Agricultural crop residues consist mainly of cellulose, hemicellulose, lignin, pectin, andother plant carbohydrates. The nature of the constituents of these residues can be best utilized as one of the five FS: Fuel, Fiber, Fertilizer, Feed and Food. Many processes have teen proposed and some are in industrial production stage. However, economics of the process depend on the location where availability of other competitive products are different.

$\beta-Galactosidase$ 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.

1. 계육사체로 NaOCL 용액에 침지시 용액중의 잔유염소농도와 coliform 및 총균수에 미치는 농도, pH, 유기산의 종류별 억제 효과를 본 결과 NaOCL 200ppm, pH3, Succinic acid의 경우가 양호하였으며 온도별 효과는 $60^{\circ}C,$ 30~60초 처리가 계육표피의 보존성이 우수하였다. 2. 저장실험에서 위와같은 조건으로 처리한 경우 $4^{\circ}C$ 저장시는 대조군에 비하여 저장이 연장되었고 $-18^{\circ}C$ 저장시 대조군에 비하여 별 유의치가 없었으나 $4^{\circ}C에서$ 해동 후 저장의 경우 대조군에 비하여 양호하였다.

Horikoshi등이 호 alkali 성 미생물에 관한 연구에서 분리한 수종의 cellulolytic bacteria중에서 가장 강력한 균체의 효소를 생산하는 Aeromonas 속 세균의 cellulolytic 효소에 관한 연구 결과를 보고한다. 공업적으로 생산된 효소를 사용하여 효소작용의 최적조건을 측정하고 gel filtration, ion-exchange chromatography 및 affinity chromatography 로 cel-luplytic 효소를 분리정제하였다. 본 효소의 활성 최적 pH는 7.0~8.5로 alkaline 효소였으며 반응온도 5$0^{\circ}C$에서 가장 강한 활성을 보였다. 분리 정제과정에서 carboxymethyl cellulose (CMC)에 대하여 활성이 있는 단백질이 최소 8종이상 분리되었으며 이중 1개 효소는 CMC에 대해서는 극히 낮은 활성을 보였으나 결정성 기질인 Avicel 에는 강한 활성을 보였다. 본 연구의 결과를 Cellulomonas속 세균 및 Trichoderma속 곰팡이의 효소와 그 성질을 비교 검토하였다.

Streptomyces속 균주가 생산하는 Phospholieste-rase를 몇가지 방법에 의하여 정제하여 그 성질을 조사 검토했다. 1) Sephadex G-50 및 DEAE-Cellulose Column Chromatography에 의하여 300배 정제하였으며 그 수율은 3.8%이었다. 2) b-PNPP을 기질로 해서 정제한 본 효소의 성질을 검토한 결과 본효소의 활성발현에 $Ca^{++}$ 이온이 필요했으며 $Ca^{++}$ 이온은 이 효소의 열안정성에도 도움을 주었다. 또 이효소의 최적작용 pH는 8.0부근이었으며 최적작용온도는 $50^{\circ}C$ 부근이었고 b-PNPP 을 기질로 한 Km 치 는 1.11mg/mι 이었다.

By employing a two-stage continuous culture system, some of important physiological parameters involved in cellulase bicsynthesis have been evalua-ted with an ultimate objective of detigning an op-timally controlled tellulase process. Volumetric and specific cellulase productivities obtained were 90 IU/liter/hr and 8IU/g biomass/hr respectively. The maximum specific enzyme productivity observed was 14.8 IU/g hiomass/hr. The optimal dilution rate in the second stage which corresponded to the maximum enzyme productivity was 0.026-0.028 hr$^{-1}$ , and the specific growth rate in the second stage ihat suported maximum specific enzyme productivity was equal to orslightly less than zero. The maintenance coefficients deter-mined for oxygen and for carbon source are M$_{o}$=0.85mmmole/g biomass/hr and M$_{c}$=0.14 mmole hexose/g bio mass/hr respectively. The yield constants determined are; Y(x/o) =32.3g biomass/mole oxygen, Y (x/c) =1.1g bio-mass/g carbon or 0.44g biomass/g hexose, Y(x/n) = 19.6g biomass/g nitrogen for the enzyme produc-tion stage and 12.5g biomass/g nitrogen for the cell growth stage.e.e.

중금속을 함유한 13종의 질산염을 명 농도별로 첨가하여 주정효모 Saccharomyces cerevisine의 주정생산과 발효작용에 미치는 영향을 조사하였다. 1. 일반적으로 중금속을 함유한 질산염은 그 첨가량이 0.0001mo1. 보다 고농도일수록 Saccharo-myces cerevisiae의 발효작용을 점차 억제하였다. 2. Nickel nitrate, chromium nitrate들의 0.0001 moi.의 첨가는 Saccharomyces cerevisiae의 alcohol 발효작용을 약간촉진시켰다. 3. Cadmium nitrate 0.001mo1. 이상, cupric nit-rate, nickel nitrate, cobalt nitrate 0.01mo1. 이상, 그리고 silver nitrate, mercurous nitrate, manganese nitrate, zinc nitrate, lead nitrate, chromiun nitrate, ferric nitrate, bismuth nitrate 0.1mol. 의 농도에서 Saccharomyces cerevisiae 의 발효작용은 완전히 조지되었다.

Acetone-dried cells of Arthrobacter simplex were entrapped in several preparations of hydrophilic urethane prepolymers and their steroid converting ability was examined. SeVeral solvents, such as methanol and propylone glycol, wereeffective for the conversion of hydrocortisone to prednisolone. The stability of the immobilized cells during storage and on repeated reactions was also examined. Thisconvenient entrapping method was also applicable for the immobilization of cellular organelles. yeast peroxisomes. The entrapped peroxi-somessh owed the activities of alcohol oxidase and catalase.