• 생약학회지
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• 제31권1호
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• pp.101-104
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• 2000

An inhibitory activity against ${\alpha}-glucosidase$ was identified in extract of an edible lichen, Umbilicaria esculenta. The inhibitor was very stable retaining above 95% of its original activity when treated with heat, acid and alkaline conditions, and some hydrolytic enzymes. Partially purified inhibitor showed strong inhibition against disaccharide hydrolytic enzymes of mammalian and mold origin, but weak or no inhibition against polysaccharide hydrolytic enzymes except glucoamylase. The inhibitor suppressed elevation of blood glucose level in rats after oral administration of soluble starch or sucrose.

• 한국미생물·생명공학회지
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• 제25권2호
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• pp.115-120
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• 1997

Penicillium sp.-L4, a causative fungus of rot in citrus fruits, was isolated and its mode of hydrolytic enzyme production was investigated. Carboxymethylcellulase (CMCase), polygalacturonase(PGase), extra- & intra-cellular $\beta$-glucosidase and cellobiase were produced drastically by addition of substrates in minimal media. Production of the hydrolytic enzymes were induced efficiently by cellobiose and cellooligosaccharides which were the products of cellulose hydrolysis, but repressed by addition of mono-saccharide such as glucose, raffinose, galacturonic acid. The relative activity of p-nitrophenyl-$\beta$-D-glucopyranoside(PNPG) hydrolysis was higher than that of cellobiose hydrolysis in extracellular enzymes, and reverse is true in intracellular enzymes. Intact enzyme production of P. sp.-L4 on lemon peel lesion was sequential. $\beta$-Glucosidase and CMCase were produced first and followed by PGase. The enzyme productivities and pH in lesions were coincident with optimal pH of each enzyme activities.

• 한국식품영양학회지
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• 제13권2호
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• pp.134-138
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• 2000

An inhibitory activity against ${\alpha}$-glucosidase was identified in extracts of medicinal lichens, Parmelia austrosinensis and P. praesorediosa. The extracts retained almost all of their original activities when treated with heat, acid and alkaline conditions, and some hydrolytic enzymes. Partially purified inhibitor showed strong inhibition against disaccharide hydrolytic enzymes of mammalian and mold origin, but weak or no inhibition against polysaccharide hydrolytic enzymes except glucoamylase. The inhibitors from the two Parmelia sp. showed almost same retention time in HPLC. The inhibitor suppressed elevation of blood glucose level in rats after oral administration of soluble starch or sucrose.

• Asian-Australasian Journal of Animal Sciences
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• 제15권12호
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• pp.1725-1731
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• 2002

The distribution and activities of hydrolytic enzymes (cellulolyti, hemicellulolytic,pectinolytic and others) in the rumen compartments of Hereford bulls fed 100% alfalfa hay based diets were evaluated. The alfalfa proportion in the diet was gradually increased for two weeks. Whole rumen contents were processed into four fractions: Rumen contents including both the liquid and solid fractions were homogenized and centrifuged, and the supernatant was assayed for enzymes located in whole rumen contents (WRE); rumen contents were centrifuged and the supernatant was assayed for enzymes located in rumen fluids (RFE); feed particles in rumen contents were separated manually, washed with buffer, resuspended in an equal volume of buffer, homogenized and centrifuged and supernatant was assayed for enzymes associated with feed particles (FAE); and rumen microbial cell fraction was separated by centrifugation, suspended in an equal volume of buffer, sonicated and centrifuged, and the supernatant was assayed for enzymes bound with microbial cells (CBE). It was found that polysaccharide-degrading proteins such as $\beta$-1,4-D-endoglucanase, $\beta$-1,4-D-exoglucanase, xylanase and pectinase enzymes were located mainly with the cell bound (CBE) fraction. However, $\beta$-D-glucosidase, $\beta$-D-fucosidase, acetylesterase, and $\alpha$-L-arabinofuranosidase were located in the rumen fluids (RFE) fraction. Protease activity distributions were 37.7, 22.1 and 40.2%, and amylase activity distributions were 51.6, 18.2 and 30.2% for the RFE, FAE and CBE fractions, respectively. These results indicated that protease is located mainly in rumen fluid and with microbial cells, whereas amylase was located mainly in the rumen fluid.

• Journal of Microbiology and Biotechnology
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• 제13권1호
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• pp.57-63
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• 2003

Using fungal (Fusarium solani f. pisi) and bacterial (Pseudomonas mendocina) cutinases, the initial hydrolysis rate of p-nitrophenyl esters was systematically estimated for a wide range of enzyme and substrate concentrations using a 96-well microplate reader. Both cutinases exhibited a high substrate specificity; i.e. a high hydrolytic activity on p-nitrophenyl butyrate (PNB), yet extremely low activity on p-nitrophenyl palmitate (PNP). When compared to the hydrolysis of PNB and PNP by other hydrolases [lipases and esterases derived from different microbial sources, such as bacteria (Pseudomonas cepacia, Psedomonas furescens, Baciilus stearothermophilus), molds (Aspeillus niger, mucor miehei), and yeasts (Candida rugosa, Candida cylindracea)], the above substrate specificity would seem to be a unique characteristic of cutinases. Secondly, the hydrolytic activity of the cutinases on PNB appeared much faster than that of the other hydrolytic enzymes mentioned above. Furthermore, the current study proved that even when the cutinases were mixed with large amounts of other hydrolases (lipases or esterases), the Initial hydrolysis rate of PNB was determined only by the cutinase concentration for each PNB concentration. This property of cutinase activity would seem to result from a higher accessibility to the substrate PNB, compared with the other hydrolytic enzymes. Accordingly, these distinct properties of cutinases may be very useful in the rapid and easy isolation of various natural cutinases with different microbial sources, each of which may provide a novel industrial application with a specific enzymatic function.

• 한국식품영양과학회지
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• 제22권3호
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• pp.273-279
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• 1993

박테리아 Bacillus sp. K-295G-7이 생산하는 두유응고효소 I 및 II에 의한 11S globulin (glycinin)의 가수분해 패턴을 조사하였다. 효소 I 과 II에 의한 acidic subunit의 응고시간은 약 4-5 분이었다. 전기 영동의 결과, acidic subunit (A$_3$, M.W=45,000)는 효소반응 2분 이내에 완전히 가수분해되어 분자량 16,000, 20,000의 새로운 band를 형성하였다. 한편 효소 II의 작용으로 약 30,000의 분자량을 가진 분해산물을 생성하였고 효소 I 과 II의 basic subunit 에 대한 가수분해 패턴은 유사하였다.

• 한국미생물·생명공학회지
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• 제48권1호
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• pp.64-71
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• 2020

A total of 262 bacterial strains were isolated from clay minerals, bentonite and zeolite, in Gyeongsangbukdo, Republic of Korea, and their hydrolytic enzyme activities were analyzed. Most of the isolated strains belonged to Micrococcales and Bacillales order. Of strains, 96 strains produced α-amylase activity, 42 strains showed cellulase activity, 111 strains had pectinase activity, and 70 strains showed protease activity. Among them, 177 isolates exhibited one or more of the hydrolytic enzyme activities and in particular Bacillus cereus MBLB1321, B. albus MBLB1326 and KIGAM017, B. mobilis MBLB1328, MBLB1329 and MBLB1330 showed all of the enzyme activities. These results demonstrate the diversity of functional Bacillus species in clay minerals as vital sources for the discovery of industrially valuable hydrolytic enzymes, which have a great commercial prospect in various bio-industrial applications.

• 한국응용곤충학회지
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• 제17권3호
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• pp.139-142
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• 1978

적성병균에 감염된 배나무 잎에서 건전부위, 병반인접부위 및 병반부위별로 몇가지 가수분해효소의 활성을 측정한 결과는 다음과 같다. 1. Cellulase (Cx), Invertase 및 $\beta-amylase$의 활성은 감염부위에서 보다 건전부위에서 더 높았고 모두 pH 7.0부근인 중성측에서 최대활성이 나타났다. 2. Pectinmethylesterase, Polygalacturonase 및 Phosphatase의 활성은 병반인접부위에서 높았다. 3. Pectinmethylesterase의 활성은 건전부위와 병반 및 그인접부위 간에 pH에 따라 심한 활성차리가 인정되었다.

• 한국미생물·생명공학회지
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• 제18권4호
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• pp.383-389
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• 1990

Penicillium verruculosum 섬유소 분해효소의 유도물질인 KC-flock 및 cellobiose octaacetate(COA)를 유일한 탄소원으로 포함하는 배지에서 21일간 배양하면서 배양여액 중의 섬유소 분해효소 각 성분의 활성도와 전기영동상의 단백질 양상을 검토하였다. 배양여액의 중의 총단백질 생성 및 섬유소 분해활성의 유도 효과는 COA 배지가 다른 두 배지의 3배 이상이었다. 배양기간의 증가에 따라 배양여액 중의 총단백질량이 증가되었는데 CMC 분해활성이나 $\beta$-glucosidase 활성의 증가보다는 avicel 분해활성도의 증가가 총단백질량의 증가와 유사하다.

• 미생물학회지
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• 제41권4호
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• pp.312-315
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• 2005

먹물버섯의 하나인 Coprinellus congregatus에서는 자실체가 성숙된 후 곧 자가분해되어 먹물로 전환된다. 이 자가분해 과정과 관련된 가수분재 효소의 역할을 이해하기 위한 첫 단계로서, 자가분해과정과 연관된 미세구조의 변화를 전자현미경으로 조사하였다. 자실체의 성숙과정에서 자실층과 자실하층에 존재하는 모든 세포질은 새로운 포자의 형성을 위하여 포자로 이동되는 것으로 보인다. 조직 내의 세포질의 고갈과 포자의 완성은 조직 내의 세포벽의 분해를 야기하는 것으로 보이며, 자실층과 자실하층의 세포벽은 동시적으로 분해 되는 것으로 생각된다. 본 연구는 먹물버섯의 자가분해가 세포질의 분해가 아닌 세포벽의 분해과정에 의한 것임을 보여 주었으며, chitin 분해효소와 같은 가수분해 효소의 중요성을 제시하였다.