• Title/Summary/Keyword: pectinolytic enzyme

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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.

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.

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.

Volatile Hazardous Compounds in Alcoholic Beverages (주류 중 휘발성 유해성분)

  • Chung, Hyun;Yoon, Mi Kyung;Kim, Meehye;Park, Sung-Kug;Lee, Joongoo;Kim, Young-Suk
    • Journal of Applied Biological Chemistry
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    • v.55 no.3
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    • pp.141-148
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    • 2012
  • Recently, concerns about the volatile hazardous compounds including acetaldehyde, methanol, and fusel oils in alcoholic beverages, which cause hangover such as headache and dizziness after consumption, have been raised. The volatile hazardous compounds might also lead to an increased incidence of liver diseases and even cancers with a high consumption of alcoholic beverages. Acetaldehyde is a volatile compound naturally found in alcoholic beverages and used as flavor in many foods. However this is also regarded as possibly being carcinogenic to humans. Furthermore, acetaldehyde with alcoholic consumption is recently classified as Group 1, carcinogenic to humans. On the other hand, methanol is generated from demethoxylation of pectin by pectinolytic enzyme during alcoholic fermentation. Higher alcohols occur naturally in alcoholic beverages as by-products of alcoholic fermentation and are generally regarded as important flavor compounds. In the current study, we reviewed on the health concern, maximum levels, analytical methods, and current levels of hazardous volatile compounds in alcoholic beverages.

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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