• 제목/요약/키워드: amylases

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Exploiting Gastrointestinal Microbes for Livestock and Industrial Development - Review -

  • Singh, Birbal;Bhat, Tej K.;Singh, Bhupinder
    • Asian-Australasian Journal of Animal Sciences
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    • 제14권4호
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    • pp.567-586
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    • 2001
  • Gastrointestinal tract of ruminants as well as monogastric animals are colonised by a variety of microorganisms including bacteria, fungi and protozoa. Gastrointestinal ecosystem, especially the rumen is emerging as an important source for enrichment and natural selection of microbes adapted to specific conditions. It represents a virtually untapped source of novel products (e.g. enzymes, antibiotics, bacteriocins, detoxificants and aromatic compounds) for industrial and therapeutic applications. Several gastrointestinal bacteria and fungi implicated in detoxification of anti-nutritional factors (ANFs) can be modified and manipulated into promising system for detoxifying feed stuffs and enhancing fibre fermentation both naturally by adaptation or through genetic engineering techniques. Intestinal lactobacilli, bifidobacteria and butyrivibrios are being thoroughly investigated and widely recommended as probiotics. Restriction endonucleases and native plasmids, as stable vectors and efficient DNA delivery systems of ruminal and intestinal bacteria, are increasingly recognised as promising tools for genetic manipulation and development of industrially useful recombinant microbes. Enzymes can improve the nutrient availability from feed stuffs, lower feed costs and reduce release of wastes into the environment. Characterization of genes encoding a variety of commercially important enzymes such as cellulases, xylanases, $\beta$-glucanases, pectinases, amylases and phytases will foster the development of more efficacious and viable enzyme supplements and enzyme expression systems for enhancing livestock production.

$\alpha$-Amylase 저해제 생산 방선균의 선별과 분류 및 $\alpha$-Amylase저해제의 분리와 Kinetics 연구 (Screening and Classification of Actinomycetes Producing $\alpha$-Amylase Inhibitors and the Isolation, their Kinetic Studies of $\alpha$-Amylase Inhibitors)

  • 김제학;김정우;김하원;심미자;최응칠;김병각
    • 한국미생물·생명공학회지
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    • 제13권3호
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    • pp.223-232
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    • 1985
  • 한국의 토양에서 분리한 균 중 bacterial $\alpha$-amylase에 저해효과가 있는 균주를 분리하여 DMC-47 균주라 명명하였고, 이 균주는 Streptomyces 속의 균임을 확인하였다. 이 균주를 옥수수 전분 배지에서 진탕 배양한 결과 4일후에 최대 저해 효과를 나타내었다. 이 균주가 생성한 저해물질은 bacterial $\alpha$-amylase, pancreatic $\alpha$-amylase, salivary $\alpha$-amylase, glucoamylase에 저해효과를 보였고, $\beta$-amylase 에는 저해효과가 없었다.

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A New α-Amylase from Reticulitermes speratus KMT1

  • Park, Han-Saem;Ham, Youngseok;Ahn, Hee-Hoon;Shin, Keum;Kim, Yeong-Suk;Kim, Tae-Jong
    • Journal of the Korean Wood Science and Technology
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    • 제42권2호
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    • pp.149-156
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    • 2014
  • Termites are wood pests that cause vast economic damage every year. They digest both cellulose and starch, but the enzymes for starch digestion have not been well characterized. We obtained complete amino acid sequence information on the KME1 ${\alpha}$-amylase from Reticulitermes speratus KMT1 through analysis of total mRNA sequences. The KME1 enzyme has two ${\alpha}$-amylase domains and is 68% identical to the ${\alpha}$-amylase from Blattellager manica, its closest relative in the GenBank database. Some unique features of its conserved region and its distant evolutionary relationship to other insect ${\alpha}$-amylases suggest that KME1 is a new type of ${\alpha}$-amylase.

과요소산 산화 전분에 의한 고구마 $\beta$-아밀라제의 수식 (Modification of Sweet Potato $\beta$-Amylase with Periodate-Oxidized Soluble Starch)

  • 안룡근;지의상
    • 한국식품영양학회지
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    • 제3권2호
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    • pp.123-132
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    • 1990
  • Sweet potato $\beta$-amylase is a tetrameric enzyme consisting of four identical polypeptide chains with a molecular weight of 5.6$\times$104, though most of the other $\beta$-amylases are monomeric enzymes. But, the relationship between subunit structure and catalytic function of the enzyme is not known. This study was done to know what the function of the subunit structure of the enzyme is. We obtained the monomer from the enzyme by the treatment of SDS, alkali pH buffer and urea. But the monomer had not activity. We tried to prepare the active monomer from the enzyme by the modification with periodate-oxidized soluble starch , In the result, we succeeded in isolating an active monomer as an oxidized soluble starch-conjugated form The active monomer had 57% of the original activity, 13.2% of the sugar and the molecular weight was estimated to be 5.4$\times$104. This results suggest that the tetrameric form of the enzyme is a most stable one and exists in nature, and the subunit structure of the enzyme Plays an important role in stabilization but not catalytic function.

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식혜의 이소말토올리고당에 관한 연구(II) -효소적 분석- (A Study on Sugars in Korean Sweet Rice Drink "Sikhye"(II) -Enzymatic Analysis of Isomaltooligosaccharides and Rice Residue-)

  • 안용근
    • 한국식품영양학회지
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    • 제10권1호
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    • pp.87-91
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    • 1997
  • 식혜에 함유된 이소말토올리고당과 밥알에 30unit/ml의 $\alpha$-아밀라아제, 글루코아밀라아제, $\alpha$-글루코시다아제, $\beta$-아밀라아제를 가하여 작용시킨 결과 글루코아밀라아제 외에는 일부밖에 가수분해하지 못하였다. 그리고, 인체의 효소인 $\alpha$-아밀라아제와 $\alpha$-글루코시다아제를 함께 작용시켜도 25% 이상 가수분해하지 못하므로 비피두스균의 활성인자로 작용할 것으로 보인다. 밥알은 물에 녹지 않기 때문에 식이섬유로도 작용할 것으로 보인다.

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한국산 곡류와 두류 중 $\alpha$-Amylase 저해물질의 검색 및 특성 (Screening and Characterization of $\alpha$-Amylase Inhibitors from Cereals and Legumes in Korea)

  • 심기환;배영일;문주석
    • 한국식품저장유통학회지
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    • 제1권2호
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    • pp.117-124
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    • 1994
  • To investigate characterization of the ${\alpha}$-amylase inhibitors from cereals and legumes produced in Korea, inhibitory activities against ${\alpha}$-amylase with the inhibitor from barley(Hordeum vulgare), wheat(Triticum aestivun), black bean(Glycine max), bean(Cajanus cajon) and pea(Pisum sativum) were measured. Among the samples tested, inhibitors from naked barley and black bean(sabong) which showed the highest inhibitor activities of cereals and legumes, respectively, were characterized according to treatment condition. The results obtained were summarized as follows. During the germination of naked barley and black bean, ${\alpha}$-amylase activities were gradually increased but inhibitory activities against ${\alpha}$-amylases were decreased. Both activities were gradually decreased when naked barley and black bean were stored. More than 50% of activities of the inhibitors from naked barley and black bean were remained at 100$^{\circ}C$ for 15 min and 20 min, respectively, indicating that the inhibitor from black bean was more stable to heat than that of barley.

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Enzymatic transformation of ginsenosides in Korean Red Ginseng (Panax ginseng Meyer) extract prepared by Spezyme and Optidex

  • Choi, Hyeon-Son;Kim, Sun Young;Park, Yooheon;Jung, Eun Young;Suh, Hyung Joo
    • Journal of Ginseng Research
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    • 제38권4호
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    • pp.264-269
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    • 2014
  • Background: In this study, we examined the effects of various enzymes on chemical conversions of ginsenosides in ginseng extract prepared by amylases. Methods: Rapidase, Econase CE, Viscozyme, Ultraflo L, and Cytolase PCL5 were used for secondary enzymatic hydrolysis after amylase treatment of ginseng extract, and ginsenoside contents, skin permeability, and chemical compositions including total sugar, acidic polysaccharide, and polyphenols were determined on the hydrolyzed ginseng extract. Results: Rapidase treatment significantly elevated total ginsenoside contents compared with the control (p < 0.05). In particular, deglycosylated ginsenosides including Rg3, which are known as bioactive compounds, were significantly increased after Rapidase treatment (p < 0.05). The Rapidase-treated group also increased the skin permeability of polyphenols compared with the control, showing the highest level of total sugar content among the enzyme treatment groups. Conclusion: This result showed that Rapidase induced the conversion of ginsenoside glycosides to aglycones. Meanwhile, Cytolase PCL5 and Econase treatments led to a significant increase of uronic acid (acidic polysaccharide) level. Taken together, our data showed that the treatments of enzymes including Rapidase are useful for the conversion and increase of ginsenosides in ginseng extracts or products.

고온성 방선균에 의한 효소생산에 관한 연구 제 1보 $\alpha$-Amylase생산균의 분이 및 효소생산 조건 (Studies on the Production of Enzymes by Thermophilic Actinomycetes Part I. Isolation and Culture Conditions of Thermostable $\alpha$-Amylase Producing Actinomycete)

  • 양한철;금범환;최용진
    • 한국미생물·생명공학회지
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    • 제3권2호
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    • pp.73-82
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    • 1975
  • In the course of studies on the production of thermostable amylases by thermophilic actinomycetes isolated from soils the investigation was carried out on the production of $\alpha$-amylase by G-1011 strain which had presented the most remarkable $\alpha$-amylase formation ability among 128 amylolytic isolates. The results were as follows : 1. Characteristics of G-1011 strain were compared with those descriptions of thermophilic actinomycetes given in Bergey's Manual. The strain was identical to these species of actinomycetes. The details of physiological properties of the strain luould he published in near future. 2. The optimum temperature for incubation of the cell growth of G-1011 strain and $\alpha$-amylase production by the strain was revealed to 5$0^{\circ}C$. 3. The effective medium for $\alpha$-amylase formation by the strain was consisted of 3.0%, soluble starch, 1.0%, peptone, 0.5%, yeast extract, 0.5%, NaCl, 0.1%, MgSO$_4$ㆍ7$H_2O$ 0.02%, $K_2$MPO$_4$and 0.002% FeSO$_4$ㆍ7$H_2O$. The pH of the medium was ajusted to 7.0 with phosphate buffer solution. 4. The maximum production of $\alpha$-amylase (3420 D. U/ml) by G-1011 strain resulted when it was grown for 16 hours with the culture of reciprocal shaking.

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Repeated Random Mutagenesis of ${\alpha}$-Amylase from Bacillus licheniformis for Improved pH Performance

  • Priyadharshini, Ramachandran;Manoharan, Shankar;Hemalatha, Devaraj;Gunasekaran, Paramasamy
    • Journal of Microbiology and Biotechnology
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    • 제20권12호
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    • pp.1696-1701
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    • 2010
  • The ${\alpha}$-amylases activity was improved by random mutagenesis and screening. A region comprising residues from the position 34-281 was randomly mutated in B. licheniformis ${\alpha}$-amylase (AmyL), and the library with mutations ranging from low, medium, and high frequencies was generated. The library was screened using an effective liquid-phase screening method to isolate mutants with an altered pH profile. The sequencing of improved variants indicated 2-5 amino acid changes. Among them, mutant TP8H5 showed an altered pH profile as compared with that of wild type. The sequencing of variant TP8H5 indicated 2 amino acid changes, Ile157Ser and Trp193Arg, which were located in the solvent accessible flexible loop region in domain B.

알긴산을 분해하는 세균 Tamlana sp. UJ94의 완전한 유전체 서열 (Complete genome sequence of Tamlana sp. UJ94 degrading alginate)

  • 정재준;배승섭;정다운;백경화
    • 미생물학회지
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    • 제54권4호
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    • pp.463-464
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    • 2018
  • Tamlana sp. UJ94는 해수로부터 분리되었으며 알긴산을 분해할 수 있다. 알긴산 분해 관련 특성을 이해하기 위해 이 세균의 유전체를 분석하였다. UJ94의 유전체는 4,116,543 bp의크기로 3,609개의 코딩서열을 가지고 있으며 35.2 mol%의 G + C 함량을 가진다. BLASTp 검색 결과 9개의 alginate lyase 외에도 6개의 agarase, 5개의 amylase, 4개의 carrageenase, 1개의 cellulase, 4개의 pectate lyase, 7개의 xylanase의 존재가 예측되어 UJ94의 다양한 다당류 분해 능력을 암시하였다. Tamlana sp. UJ94의 유전체는 생물전환 공정에 사용할 수 있는 다당류 분해 유전자를 제공할 수 있을 것이다.