• Title/Summary/Keyword: pectinolytic activity

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Enzyme Production Related to Alcohol Metabolism from Thermophilic Fungus Thermoascus aurantiacus (호열성 사상균 Thermoascus aurantiacus의 알코올분해대사 관련 효소학적 특성)

  • Ko Hee-Sun;Kim Hyun-Soo
    • Microbiology and Biotechnology Letters
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    • v.34 no.3
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    • pp.216-220
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    • 2006
  • Thermophillic fungus Thermoascus aurantiacus showed excellent growth and produced high amount of alcohol oxidase and catalase in a pectin medium. Besides, the strain produced enzymes which related with pectin or alcohol decomposition. We detected extracellular pectin esterase (EC 3.1.1.11) activity and, both intracellular and extracellular pectinase (EC 4.2.2.10) activity, as pectinolytic enzymes produced by T. aurantiacus. The production of methanol decomposition enzymes, such as alcohol oxidase (AOD, EC 1.1.3.13), alcohol dehydrogenase (ADH, EC 1.1.1.1), formaldehyde dehydrogenase (FADH, EC 1.2.1.1) and formate dehydrogenase (FDH, EC 1.2.1.2) follows by pectin esterase reaction which is converted to methanol. We concluded that T. aurantiacus has pectinolytic and alcohol - oxidative enzymological mechanism which produced carbon dioxide as a final material, started from pectin.

Collection and Identification of Molds from Citrus Oranges during Post-Harvest Storage (온주밀감 부패 곰팡이의 분리 및 동정)

  • Ko, Young-Hwan;Kim, Se-Jae
    • Korean Journal of Food Science and Technology
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    • v.28 no.6
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    • pp.1142-1145
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    • 1996
  • Long term-storage of citrus oranges after harvest has been hindered mainly by molds The goal of this research was to collect and identify those molds, which would help find a way to extend shelf-life after harvest. During the period of 1994 to 1995, fourteen different strains were isolated and purified from putrefied fruit (Citrus unshiu var.) that was stored at room temperature under open air. The storage disease was caused by the following molds: Penicillium italicum, 25.8%, Monilia candida, 19.8%; Alternaria citri, 18.1%; Mucor hiemalis, 11.0%; Phomopsis citri, 6.6%; Botrytis cinerea. 5.5%; Phoma citricarpa, 3.8%; Glomerella cingulata, 3.8%; P. digitatum, 1.1%; other molds, 4.5%; Most of the strains showed pectinolytic activity and putrefaction. These citrus fruit-putrefying molds will be used as target strains for the control of microorganisms during post-harvest storage.

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Prevention of Pectinolytic Softening of Kimchi Tissue (펙틴 분해효소를 이용한 김치 조직의 연화 방지)

  • Baek, Hyung-Hee;Lee, Chang-Hee;Woo, Duk-Hyun;Park, Kwan-Hwa;Pek, Un-Hwa;Lee, Kyu-Soon;Nam, Sang-Bong
    • Korean Journal of Food Science and Technology
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    • v.21 no.1
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    • pp.149-153
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    • 1989
  • Polygalacturonase(PG) and pectinesterase(PE) were extracted from Chinese cabbage and physicochemical properties of the enzymes were characterized. The preheating conditions for maximum retention of Kimchi texture were also studied. The activity of PE was highest at $50^{\circ}C$ and at 0.02M $CaCl_2$ but decreased in 0.2M $CaCl_2$, PG exhibited maximum activity at $65^{\circ}C$ with 0.3mM $CaCl_2$ but was inhibited by $CaCl_2$ at 0.5mM. Both of the enzymes, however, exhibited the maximum activity with 0.25M NaCl. Optimum preheating treatment was determined for minimum PG activity and maximum PE activity. Thus a maximum crispness and firmness was obtained with preheating in 0.05M $CaCl_2$ solution at $50^{\circ}C$ for 1.5hr results indicated that PE activity and calcium ion were very effective in preserving firmness.

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Statistical Optimization of the Medium Components for the Production of Protopectinases by Bacillus subtilis

  • Shahbazian, Nafise;Ashtiani, Farzin Zokaee;Bonakdarpour, Babak
    • Food Science and Biotechnology
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    • v.18 no.2
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    • pp.442-448
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    • 2009
  • In this study Bacillus subtilis PTCC 1023 was used for the production of protopectinase using soybean based media. The use of isolated soybean protein (ISP) and soybean flour resulted in similar protopectinase production and growth rates. The effect of medium composition on protopectinase production was studied using central composite design (CCD) methodology. The change in the concentration of ISP (1-7%), glucose (0-10%), and phosphate (0.1-0.3 M) was found to affect the protopectinase activity (response variable) after 24 hr of cultivation. In the range studied, ISP and glucose had a negative effect on the response variable, whereas phosphate had a positive effect. A statistically significant interaction was identified between phosphate and ISP, suggesting that correct optimization of medium formulation in this case can only be obtained using factorial design of experiments. Protopectinase activity exceeding 215 U/mL was obtained in a medium containing 4% ISP, 0.3M phosphate, and no added sugar.

Taxonobic Characteristics of Strain Producing MR-387A and B,New Inhibitors of Aminopeptidase M,and their Production (신규의 Aminopeptidase M 저해제 MR-387A와 B를 생산하는 균주의 동정 및 저해제의 생산)

  • Chung, Myung-Chul;Chun, Hyo-Kon;Lee, Ho-Jae;Kho, Yung-Hee
    • Microbiology and Biotechnology Letters
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    • v.22 no.5
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    • pp.447-452
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    • 1994
  • The strain SL-387 which produces new inhibitors of aminopeptidase M, MR-387A and B, was isolated from a soil sample. The strain has branched substrate mycelia, from which aerial hyphae develop in the form of open spirals. Spore surface is smooth. Melanoid and soluble pigme- nts were observed. The isolate contains LL-diaminopimelic acid in its cell wall hydrolysate, and has no pectinolytic activity. The strain SL-387 is closely related to Streptomyces griseoruber and S. naganishii, but is different from these strains in some cultural and physiological characteristics. This strain was, therefore, designated as Streptomyces sp. SL-387. The effects of several carbon and nitrogen sources on the production of the inhibitor were examined. Among them, glucose, galactose, mannose, and xylose were effective as a carbon source and soybean meal, soytone, fish meal, and gluten meal were effective as a nitrogen source. The maximum peak of the inhibitor production in jar fermentor was obtained on the fifth day of culture.

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Distribution and Activities of Hydrolytic Enzymes in the Rumen Compartments of Hereford Bulls Fed Alfalfa Based Diet

  • Lee, S.S.;Kim, C.-H.;Ha, J.K.;Moon, Y.H.;Choi, N.J.;Cheng, K.-J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.15 no.12
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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.

A Review of Interactions between Dietary Fiber and the Gastrointestinal Microbiota and Their Consequences on Intestinal Phosphorus Metabolism in Growing Pigs

  • Metzler, B.U.;Mosenthin, R.
    • Asian-Australasian Journal of Animal Sciences
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    • v.21 no.4
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    • pp.603-615
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    • 2008
  • Dietary fiber is an inevitable component in pig diets. In non-ruminants, it may influence many physiological processes in the gastrointestinal tract (GIT) such as transit time as well as nutrient digestion and absorption. Moreover, dietary fiber is also the main substrate of intestinal bacteria. The bacterial community structure is largely susceptible to changes in the fiber content of a pig's diet. Indeed, bacterial composition in the lower GIT will adapt to the supply of high levels of dietary fiber by increased growth of bacteria with cellulolytic, pectinolytic and hemicellulolytic activities such as Ruminococcus spp., Bacteroides spp. and Clostridium spp. Furthermore, there is growing evidence for growth promotion of beneficial bacteria, such as lactobacilli and bifidobacteria, by certain types of dietary fiber in the small intestine of pigs. Studies in rats have shown that both phosphorus (P) and calcium (Ca) play an important role in the fermentative activity and growth of the intestinal microbiota. This can be attributed to the significance of P for the bacterial cell metabolism and to the buffering functions of Ca-phosphate in intestinal digesta. Moreover, under P deficient conditions, ruminal NDF degradation as well as VFA and bacterial ATP production are reduced. Similar studies in pigs are scarce but there is some evidence that dietary fiber may influence the ileal and fecal P digestibility as well as P disappearance in the large intestine, probably due to microbial P requirement for fermentation. On the other hand, fermentation of dietary fiber may improve the availability of minerals such as P and Ca which can be subsequently absorbed and/or utilized by the microbiota of the pig's large intestine.

Characterization of Pectinolytic Enzyme and Blanching Condition of Raw Carrots (당근의 펙틴 분해효소 특성 및 예비열처리 조건)

  • 이현규;이경숙;이상화;최은옥;바관화
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.30 no.2
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    • pp.228-233
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    • 2001
  • This study was carried out to characterize the enzymatic properties and effectiveness on the firmness of pectinesterase(PE) and polygalacturonase(PG) which are present in carrot cell wall, and to determine the blanching condition of raw carrot. Crude enzyme was extracted from carrots and used as PE and PG. The optimum pH of PE and PG activity were 7.0 and 5.0, respectively. NaCl enhanced PE and PG activities, particularly at 0.15 M and 0.10 M, respectively. Although the optimum temperature of PG ($70^{\circ}C$) was higher than that of PE ($50^{\circ}C$), PE ($Z-value=8.76^{\circ}C$) was more heat-stable than PG($Z-value=6.67^{\circ}C$). Blanching condition was determined as at $55^{\circ}C$ for 60 min in 0.03 M $CaCl_2$, 0.1 M NaCl and pH 7.0 from measuring firmness after blanching at various temperature ($50~70^{\circ}C$) and time (5~60 min).

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