• Title/Summary/Keyword: cellulase activities

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Fungal Strain Improvement for Cellulase Production Using Repeated and Sequential Mutagenesis

  • Vu, Van-Hanh;Pham, Tuan-Anh;Kim, Keun
    • Mycobiology
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    • v.37 no.4
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    • pp.267-271
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    • 2009
  • A fungal strain producing a high level of cellulase was selected from 320 fungal isolates and identified as Aspergillus sp. This strain was further improved for cellulase production by sequential treatments by two repeated rounds of $\gamma$-irradiation of $Co^{60}$, ultraviolet treatment and four repeated rounds of treatment with N-methyl-N'-nitro-N-nitrosoguanidine. The best mutant strain, Aspergillus sp. XTG-4, was selected after screening and the activities of carboxymethyl cellulase, filter paper cellulase and $\beta$-glucosidase of the cellulase were improved by 2.03-, 3.20-, and 1.80-fold, respectively, when compared to the wild type strain. After being subcultured 19 times, the enzyme production of the mutant Aspergillus sp. XTG-4s was stable.

The Cellulase and Pectinase Activities Associated with the Virulence of Indigenous Sclerotinia sclerotiorum Isolates in Jordan Valley

  • Asoufi, H.;Hameed, K.M.;Mahasneh, A.
    • The Plant Pathology Journal
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    • v.23 no.4
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    • pp.233-238
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    • 2007
  • Twenty five isolates of Sclerotinia sclerotiorum were recovered from different infested fields of vegetable along the heavily cultivated crops in Jordan valley. Cellulase and pectinase activities of those isolates were detected using CMC and pectin agar media, respectively. Diameter of the clearing zones on those media represented the level of such enzymatic activities, characteristic of each isolate. The virulence of those isolates was studied using a squash (Cucurbita pipo) cultivar under a greenhouse condition. The significance of correlating the enzymatic activity with the virulence of the isolates was ascertained and discussed.

The changes in the activities of Cellulase and Xylanase of Aspergillus phoenicis during the life cycle (Aspergillus phoenicis의 生活史를 통한 Cellulase 및 Xylanase의 活性 변화)

  • Oh, Chan-Seok;Lee, Yung-Nok
    • Korean Journal of Microbiology
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    • v.22 no.2
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    • pp.91-96
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    • 1984
  • The changes in the activities of Cellulase and Xylanase of A. phoencis during the life cycle were surveyed by using synchronized culture technique. Avicelase activity of the fungus was reached at peak in the initial hyphal growth stage, but decreased gradually during the conidiophore formation, vesicle-phialide formation, and sporulation stages in decreasing order. CMCase, Salicinase, and Xylanase activities were raised very high in the initial hyphal growth stage, but decreased gradually in conidiophore formation and vesicle-phialide formation stages, and then increased, more or less, in the sporulation stage.

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Studies on The Microbial Utilization of Agricultural Wastes (Part 5) Isolation and Selection of Cellulase Producing Fungi (농산폐자원의 미생물학적 이용에 관한 연구 (제오보) 섬유소분해효소 생산 곰팡이의 분리 및 선별)

  • Bae, Moo;Kim, Byung-Hong;Lee, Gye-Jun
    • Microbiology and Biotechnology Letters
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    • v.4 no.3
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    • pp.105-110
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    • 1976
  • In the studies of microbiological utilization of cellulosic wastes, cellulolytic fungi were isolated and screened out. At the first stage, 221 cellulolytic fungi were isolated from different sources such as soils, humus, composts and rotten wood debris by enrichment culture techniques. In the second stage, 36 strains of fungi out of those previously isolated were selected for their cellulase activities estimated by means of filter paper degradation, carboxy methyl cellulose liquefaction and cup method. Activities of C$_1$-cellulase, C$\sub$x/-cellulase and filter paper activity were adopted on the final screening stage and five different strains which are tentatively identified as Aspergillus sp.(strain No. AS-9), Penicillium sp. (strain No. KNI-1-2), Trichoderma, sp. (strain No. KI-7-2, KI-7-5, KI-4-1-1B) were selected for their high potency of C$_1$ and C$\sub$x/-cellulase activities. When rice straw milled and treated with NH$_4$OH was hydrolyzed with the crude enzyme Prepared from the culture broth of Trichoderma sp. (strain No. KI-4-1-1B), saccharification rate was obtained up to 26%.

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Metagenome Analysis of Protein Domain Collocation within Cellulase Genes of Goat Rumen Microbes

  • Lim, SooYeon;Seo, Jaehyun;Choi, Hyunbong;Yoon, Duhak;Nam, Jungrye;Kim, Heebal;Cho, Seoae;Chang, Jongsoo
    • Asian-Australasian Journal of Animal Sciences
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    • v.26 no.8
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    • pp.1144-1151
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    • 2013
  • In this study, protein domains with cellulase activity in goat rumen microbes were investigated using metagenomic and bioinformatic analyses. After the complete genome of goat rumen microbes was obtained using a shotgun sequencing method, 217,892,109 pair reads were filtered, including only those with 70% identity, 100-bp matches, and thresholds below $E^{-10}$ using METAIDBA. These filtered contigs were assembled and annotated using blastN against the NCBI nucleotide database. As a result, a microbial community structure with 1431 species was analyzed, among which Prevotella ruminicola 23 bacteria and Butyrivibrio proteoclasticus B316 were the dominant groups. In parallel, 201 sequences related with cellulase activities (EC.3.2.1.4) were obtained through blast searches using the enzyme.dat file provided by the NCBI database. After translating the nucleotide sequence into a protein sequence using Interproscan, 28 protein domains with cellulase activity were identified using the HMMER package with threshold E values below $10^{-5}$. Cellulase activity protein domain profiling showed that the major protein domains such as lipase GDSL, cellulase, and Glyco hydro 10 were present in bacterial species with strong cellulase activities. Furthermore, correlation plots clearly displayed the strong positive correlation between some protein domain groups, which was indicative of microbial adaption in the goat rumen based on feeding habits. This is the first metagenomic analysis of cellulase activity protein domains using bioinformatics from the goat rumen.

Acanthophysium sp. KMF001, a New Strain with High Cellulase Activity

  • YOON, Sae-Min;PARK, So-Hyun;KIM, Tea-Jong;KIM, Young-Kyoon;KIM, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • v.47 no.6
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    • pp.751-760
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    • 2019
  • Cellulase is an eco-friendly biocatalyst, and its demand is growing in many industrial applications such as food, textile, paper, and bioenergy. Strains with a high cellulase activities are the starting point for the economic production of cellulase. In a previous study, Acanthophysium sp. KMF001 with high cellulase production ability was selected among 54 wood-rotting fungi. In this study, we evaluated the cellulase productivity of Acanthophysium sp. KMF001 quantitatively and analyzed its taxonomic location using a genetic method. Acanthophysium sp. KMF001 showed high cellulase productivity similar to that of Acanthophysium bisporum and was much better than A. bisporum in specific enzyme activity. The 28S rRNA sequence of Acanthophysium sp. KMF001 was similar to that of Acanthophysium lividocaeruleum MB1825, with 98.40% homology. Phylogenetic analysis suggested that Acanthophysium sp. KMF001 is a new strain. In this study, we propose a new strain with high cellulase productivity.

Production of Cellulase by Trichoderma reesei Rut C30 in Wheat Bran-containing Media

  • Yu, Xiao-Bin;Yun, Hyun-Shik;Koo, Yoon-Mo
    • Journal of Microbiology and Biotechnology
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    • v.8 no.3
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    • pp.208-213
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    • 1998
  • The effect of the addition of wheat bran to the growth medium on the production of cellulolytic enzymes of Trichoderma reesei Rut C30 was studied in batch culture using shake flasks. The activity of cellulase was enhanced by the addition of wheat bran to the cellulase production medium. $KH_2PO_4$-$K_2HPO_4$ buffer was used for pH control during cellulase production. As a result, high cellulase activities were obtained in shake flask culture; a CMC (carboxymethyl cellulose) activity of 125.78 U/ml was obtained from 2% Avicel- and 3% wheat bran-containing medium and an FP (filter paper) activity of 12.85U/ml was obtained from 1% Avicel- and 5% wheat bran-containing medium after 6 days of cultivation.

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Construction of bifunctional xylanase-cellulase fusion protein from Bacillus licheniformis NBL420 and its expression in E. coli (Bacillus licheniformis NBL420 유래의 Xylanase-Cellulase 활성을 갖는 융합단백질 제작과 대장균에서의 발현)

  • Hong, In-Pyo;Choi, Shin-Geon
    • Journal of Industrial Technology
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    • v.29 no.A
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    • pp.161-167
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    • 2009
  • The bifunctional Xylanase-Cellulase hybrid protein was constructed by gene fusion. Two genes corresponding to endoxylanase gene (xylS) and endocellulase gene (celA) were amplified by PCR from Bacillus licleniformis NBL420. It was then linked through splicing by overlap extension (SOE) by PCR method. The two resulting fused hybrids, xyl/cel and cel/xyl, which differ by its orientation, were confirmed by its nucleotide sequencings. One of two fusion genes, xyl/cel was successfully expressed into pET22b(+) vector (pxyl/cel) with bifunctional xylanase-cellulase activity. On the contrary, the other cel/xyl fusion protein showed only cellulase activity with much decreased xylanase activity. Enzymatic properties of Xyl/Cel fusion protein were investigated regarding optimum pH, optimum temp, thermostability, and pH stability. It was revealed that Xyl/Cel fusion protein retained the bifunctional xylanase-cellulase activities eventhough two enzymes were connected with each other directly. These informations could be useful for construction of other hybrid proteins as well as increased range of substrate utilization.

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Production of Cellulase from Lignocellulosic Waste. (리그노셀룰로스계 폐기물을 이용한 Cellulase의 생산)

  • 강성우;이진석;김승욱
    • Microbiology and Biotechnology Letters
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    • v.30 no.1
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    • pp.98-102
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    • 2002
  • Lignocellulosic wastes available in abundance can be excellent substrates for the production of cellulase. Different types of substrates and various pretreatments were used to improve the production of cellulase. The steam-exploded wood chip gave the highest activities of FPase (0.84 IU/mL) and CMCase (6.5 IU/mL) in the shake-flask culture. In 30 L bioreactor the steam-exploded wood chip and residue after saccharification gave the FPase activity (0.72 IU/mL) and the CMCase activity (6.3 IU/mL), respectively, similar those obtained in lactose.

Cytochemical Study on the Cellulase Activity in the Digestive System of a Land Snail Helix aspersa

  • Jeong, Kye-Heon;Lee, Yong-Seok
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2000.05a
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    • pp.539-539
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    • 2000
  • A cytochemical study by the Benedict's reaction method was conducted to find out the cellulase activity in the digestive organs of Helix aspersa. Out of the all digestive organs, the stomach, the intestine, and the digestive gland showed cellulase activities under the transmission electron microscopy.

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