Monitoring the Activity of Different Trichoderma Isolates by the Isoelectric Points (pI) of Their Extracellular Enzymes

The extracellular enzyme proteins secreted by Sporotrichum (Chrysosporium) thermophile, ATCC 42 464, upon growth on cellulose or cellobiose, were separated by polyacrylamide gel electrophoresis and electrofocusing into different fractions which were then analyzed with respect to their enzymatic character to identify the cellulolytic enzymes. A positive reaction against carboxymethylcellulose azure (CMC azure) was taken as evidence for an endo-acting cellulase, whereas the criterion for the presence of an exo-cellulase was a negative reaction with CMC azure and a concomitant increase in reducing power upon action of any kind of cellulose. With this procedure, four main cellulolytic enzymes were detected: three endo-cellulases, named endo-cellulases I, II, and III (with corresponding isoelectric points 5.1, 4.2, 5.7), and an exo-cellulase (isoelectric point 4.7). With respect to their enzymatic action on amorphous cellulose, endo-cellulases I and III were isofunctional, releasing cellobiose and cellodextrins as hydrolytic products, whereas endo-cellulase II was found to produce additionally some glucose. Endo-cellulases I and III were also able to attack native (crystalline) cellulose like filter paper or Avicel, but endo-cellulase II could not and thus behaved as a true carboxymethylcellulase. The rate of formation of endo-cellulase I during growth was distinctly superior from that of the other cellulases so that the proportion of the activity due to endo-cellulase. I compared with that due to the others constantly increased during the culture.

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Cultural conditions on the production of extracellular enzymes by Trichoderma isolates from tobacco rhizosphere

Brazilian Journal of Microbiology ◽

10.1016/j.bjm.2015.11.007 ◽

2016 ◽

Vol 47 (1) ◽

pp. 25-32 ◽

Cited By ~ 5

Author(s):

K.L.N. Mallikharjuna Rao ◽

K. Siva Raju ◽

H. Ravisankar

Keyword(s):

Extracellular Enzymes ◽

Cultural Conditions ◽

Trichoderma Isolates

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The Hierarchic Order of Intermediate Filament Structure and Assembly

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100120308 ◽

1985 ◽

Vol 43 ◽

pp. 722-725

Author(s):

U. Aebi ◽

E.C. Glavaris ◽

R. Eichner

Keyword(s):

Tissue Specificity ◽

Structural Model ◽

Eukaryotic Cells ◽

Cdna Sequencing ◽

Filament Structure ◽

Keratin Filaments ◽

Isoelectric Points ◽

Immunological Crossreactivity

Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.

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Molecular reidentification of human pathogenic Trichoderma isolates as Trichoderma longibrachiatum and Trichoderma citrinoviride

Medical Mycology ◽

10.1046/j.1365-280x.1999.00197.x ◽

1999 ◽

Vol 37 (1) ◽

pp. 25-33 ◽

Cited By ~ 2

Author(s):

K. KUHLS ◽

E. LIECKFELDT ◽

T. BORNER ◽

E. GUEHO

Keyword(s):

Trichoderma Longibrachiatum ◽

Trichoderma Citrinoviride ◽

Trichoderma Isolates

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Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657116 ◽

1982 ◽

Vol 47 (01) ◽

pp. 019-021 ◽

Cited By ~ 13

Author(s):

Cemal Kuyas ◽

André Haeberli ◽

P Werner Straub

Keyword(s):

Sialic Acid ◽

Polypeptide Chain ◽

Two Dimensional ◽

Charge Heterogeneity ◽

Human Fibrinogen ◽

Two Dimensional Electrophoresis ◽

Isoelectric Points ◽

Polypeptide Chains ◽

Dimensional Electrophoresis ◽

Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

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Profiling of Intra- and Extracellular Enzymes Involved in Fructification of the Lingzhi or Reishi Medicinal Mushroom, Ganoderma lucidum (Agaricomycetes)

International Journal of Medicinal Mushrooms ◽

10.1615/intjmedmushrooms.2018028898 ◽

2018 ◽

Vol 20 (12) ◽

pp. 1209-1221

Author(s):

Anna Goyal ◽

Anu Kalia ◽

Harpreet Singh Sodhi

Keyword(s):

Ganoderma Lucidum ◽

Extracellular Enzymes ◽

Medicinal Mushroom

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Aspergillus sydowii Strain SCAU066 and Aspergillus versicolor Isolate BAB-6580: Potential Source of Xylanolytic, Cellulolytic and Amylolytic Enzymes

Science Letters ◽

10.24191/sl.v14i2.9539 ◽

2020 ◽

Vol 14 (2) ◽

pp. 15

Author(s):

Zaidah Zainal ariffin

Keyword(s):

Extracellular Enzymes ◽

Biologically Active ◽

Aspergillus Versicolor ◽

Aspergillus Sydowii ◽

Aspergillus Tamarii ◽

Alternative Source ◽

Amylolytic Enzymes ◽

Potato Dextrose Broth ◽

Wide Range ◽

Pharmaceutical Industries

Fungi is known to produce a wide range of biologically active metabolites and enzymes. Enzymes produced by fungi are utilized in food and pharmaceutical industries because of their rich enzymatic profile. Filamentous fungi are particularly interesting due to their high production of extracellular enzymes which has a large industrial potential. The aim of this study is to isolate potential soil fungi species that are able to produce functional enzymes for industries. Five Aspergillus species were successfully isolated from antibiotic overexposed soil (GPS coordinate of N3.093219 E101.40269) by standard microbiological method. The isolated fungi were identified via morphological observations and molecular tools; polymerase chain reactions, ITS 1 (5’- TCC GTA GGT GAA CCT GCG G3’) forward primer and ITS 4 (5’-TCC TCC GCT TAT TGA TAT GC-3’) reverse primer. The isolated fungi were identified as Aspergillus sydowii strain SCAU066, Aspergillus tamarii isolate TN-7, Aspergillus candidus strain KUFA 0062, Aspergillus versicolor isolate BAB-6580, and Aspergillus protuberus strain KAS 6024. Supernatant obtained via submerged fermentation of the isolated fungi in potato dextrose broth (PDB) and extracted via centrifugation was loaded onto specific media to screen for the production of xylanolytic, cellulolytic and amylolytic enzymes. The present findings indicate that Aspergillus sydowii strain SCAU066 and Aspergillus versicolor isolate BAB-6580 have great potential as an alternative source of xylanolytic, cellulolytic and amylolytic enzymes.

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