scholarly journals Characterization of the cellulolytic activity of a Bacillus isolate.

1984 ◽  
Vol 47 (5) ◽  
pp. 1039-1046 ◽  
Author(s):  
L M Robson ◽  
G H Chambliss
2020 ◽  
Vol 21 (10) ◽  
Author(s):  
Ari Hepi Yanti ◽  
Tri Rima Setyawati ◽  
Rikhsan Kurniatuhadi

Abstract. Yanti AH, Setyawati TR, Kurniatuhadi R. 2020. Isolation and characterization of lactic acid bacteria from fecal pellets, coelomic fluid, and gastrointestinal tract of Nypa worm (Namalycastis rhodochorde) from West Kalimantan, Indonesia. Biodiversitas 21: 4726-4731. Lactic acid bacteria isolated from the intestinal tract as probiotic could be beneficial because they could trigger the growth of the host by enhancing digestibility, increasing their immune system, and inhibiting pathogenic bacteria through the enzymatic process or metabolites production. The purposes of this study were to identify and characterize lactic acid bacteria from fecal pellets, coelomic fluid, and gastrointestinal tract of Nypa worm (Namalycastis rhodochorde). Bacterial isolation was carried out by the pour plate method on de Mann Rogosa Sharp Agar (MRSA). Lactic Acid Bacteria (LAB) isolates were purified and then physiologically characterized by some biochemical tests. Cellulolytic activities were carried out by detecting a clear zone formation on CMC-congo Red Agar. There were 20 isolates of lactic acid bacteria from fecal pellets, coelom fluid, and gastrointestinal tract of nypa worm. Ten isolates (50%) had cellulolytic activity on CMC-phenol red agar. Eight isolates were closely related to the genus Lactobacillus, while two isolates were closely related to the genus Bacillus. These cellulolytic bacteria could be developed further as probiotic in Nypa worm feed.


Author(s):  
Jonathan D. Willis ◽  
William E. Klingeman ◽  
Cris Oppert ◽  
Brenda Oppert ◽  
Juan L. Jurat-Fuentes

2016 ◽  
Vol 15 (3) ◽  
Author(s):  
A.F.N. Volpini ◽  
T. Thomazine ◽  
S.H. Umeo ◽  
G.A. Pereira ◽  
G.A. Linde ◽  
...  

2004 ◽  
Vol 20 (8) ◽  
pp. 837-843 ◽  
Author(s):  
C. Ganesh Kumar ◽  
Han-seung Joo ◽  
Rajesh Kavali ◽  
Jang-won Choi ◽  
Chung-soon Chang
Keyword(s):  

2019 ◽  
Vol 47 (3) ◽  
Author(s):  
Gamal El-BAROTY ◽  
Faten ABOU-ELELLA ◽  
Hassan MOAWAD ◽  
Talaat N. El-SEBAI ◽  
Fatma ABDULAZIZ ◽  
...  

Since accumulation of agricultural wastes represents a huge problem, it was important to explore the available methods to help eliminate agricultural wastes safely, and simultaneously produce functional enzyme like cellulase. Six native Egyptian fungal strains were isolated, morphologically identified and screened for cellulose biodegradation potential, which was determined as endoglucanase or as carboximethylcellulase (CMCase). The most promising isolate (Aspergillus terreus) was selected for molecular characterizations based on sequencing of internal transcribed spacer (ITS). Further optimization experiments were accomplished on the selected strain. The strain with cellulolytic activity, 2.26 IU mL-1 was identified using ITS nucleotides (genes) sequences and the result confirmed that the strain is 99.8% homology with A. terreus. Then, it was submitted to GeneBank and given an accession number. Further optimization experiments revealed that 35ºC is the optimum temperature for cellulase production and raised the enzyme activity (EA) up to 3.19 IU mL-1. Out of two organic nitrogen sources; peptone at concentration 6 gL-1 was found to be the optimum nitrogen source for cellulase production with the highest activity 4 IU mL-1. Whereas, the different four carbon sources: microcellulose, corn stalks, wheat straw and rice straw showed significant differences in EA with values 11.07, 9.68, 7.87 and 3.71 IU mL-1, respectively at  pH 3. The maximum EA was recorded to be within 5-7 days of incubation, dependent on type of carbon sources. The optimization of different incubation conditions raised cellulolytic activity from 2.26 IU mL-1 up to 11.18 IU mL-1.   ********* In press - Online First. Article has been peer reviewed, accepted for publication and published online without pagination. It will receive pagination when the issue will be ready for publishing as a complete number (Volume 47, Issue 3, 2019). The article is searchable and citable by Digital Object Identifier (DOI). DOI link will become active after the article will be included in the complete issue. *********


1971 ◽  
Vol 17 (1) ◽  
pp. 31-37 ◽  
Author(s):  
R. E. Smith ◽  
T. S. Neudoerffer

A bacterial contaminant from a cellulase-producing culture of Trichurus cylindricus was subjected to physiological and biochemical tests, and identified as a member of the genus Micrococcus, subgroup 6 (Baird-Parker). It appeared either to stimulate cellulase production by the fungus, or to increase cellulase activity. The amino acid and protein content of the Micrococcus suggested that it might be useful as a feed supplement. In a preliminary trial, rats accepted freeze-dried cells as a partial source of energy, and grew at a normal rate. No toxic effects of the diet were noted.


2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Søren Brander ◽  
Stine Lausten ◽  
Johan Ø. Ipsen ◽  
Kristoffer B. Falkenberg ◽  
Andreas B. Bertelsen ◽  
...  

Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are important industrial enzymes known for their catalytic degradation of recalcitrant polymers such as cellulose or chitin. Their activity can be measured by lengthy HPLC methods, while high-throughput methods are less specific. A fast and specific LPMO assay would simplify screening for new or engineered LPMOs and accelerate biochemical characterization. Results A novel LPMO activity assay was developed based on the production of the dye phenolphthalein (PHP) from its reduced counterpart (rPHP). The colour response of rPHP oxidisation catalysed by the cellulose-specific LPMO from Thermoascus aurantiacus (TaAA9A), was found to increase tenfold by adding dehydroascorbate (DHA) as a co-substrate. The assay using a combination of rPHP and DHA was tested on 12 different metallo-enzymes, but only the LPMOs catalysed this reaction. The assay was optimized for characterization of TaAA9A and showed a sensitivity of 15 nM after 30 min incubation. It followed apparent Michaelis–Menten kinetics with kcat = 0.09 s−1 and KM = 244 µM, and the assay was used to confirm stoichiometric copper–enzyme binding and enzyme unfolding at a temperature of approximately 60 °C. DHA, glutathione and fructose were found to enhance LPMO oxidation of rPHP and in the optimized assay conditions these co-substrates also enabled cellulose degradation. Conclusions This novel and specific LPMO assay can be carried out in a convenient microtiter plate format ready for high-throughput screening and enzyme characterization. DHA was the best co-substrate tested for oxidation of rPHP and this preference appears to be LPMO-specific. The identified co-substrates DHA and fructose are not normally considered as LPMO co-substrates but here they are shown to facilitate both oxidation of rPHP and degradation of cellulose. This is a rare example of a finding from a high-throughput assay that directly translate into enzyme activity on an insoluble substrate. The rPHP-based assay thus expands our understanding of LPMO catalysed reactions and has the potential to characterize LPMO activity in industrial settings, where usual co-substrates such as ascorbate and oxygen are depleted.


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