Potential of Thermophilic Fungus Rhizomucor pusillus NRRL 28626 in Biotransformation of Antihelmintic Drug Albendazole

2011 ◽  
Vol 165 (5-6) ◽  
pp. 1120-1128 ◽  
Author(s):  
G. Shyam Prasad ◽  
S. Girisham ◽  
S. M. Reddy
Keyword(s):  
Thermophilic Fungus ◽  
Rhizomucor Pusillus

Phytase production by the thermophilic fungus Rhizomucor pusillus

2004 ◽  
Vol 20 (1) ◽  
pp. 105-109 ◽  
Author(s):  
B.S. Chadha ◽  
Gulati Harmeet ◽  
Minhas Mandeep ◽  
H.S. Saini ◽  
N. Singh
Keyword(s):  
Thermophilic Fungus ◽  
Phytase Production ◽  
Rhizomucor Pusillus

Amylase hyperproduction by deregulated mutants of the thermophilic fungus Thermomyces lanuginosus

2002 ◽  
Vol 29 (2) ◽  
pp. 70-74
Author(s):  
K Rubinder ◽  
BS Chadha ◽  
N Singh ◽  
HS Saini ◽  
S Singh
Keyword(s):  
Thermophilic Fungus ◽  
Thermomyces Lanuginosus

scholarly journals Fulminant Rhizomucor pusillus mucormycosis during anti-leukemic treatment with blinatumomab in a child: A case report and review of the literature

2020 ◽  
Author(s):  
Sarah Schober ◽  
Karin Melanie Cabanillas Stanchi ◽  
Anna Riecker ◽  
Matthias Pfeiffer ◽  
Ilias Tsiflikas ◽  
...  
Keyword(s):  
Case Report ◽  
Review Of The Literature ◽  
Rhizomucor Pusillus

Comparative biocontrol ability of chitinases from bacteria and recombinant chitinases from the thermophilic fungus Thermomyces lanuginosus

2019 ◽  
Vol 127 (6) ◽  
pp. 663-671 ◽  
Author(s):  
Ruth Nyanduko Okongo ◽  
Adarsh Kumar Puri ◽  
Zhengxiang Wang ◽  
Suren Singh ◽  
Kugen Permaul
Keyword(s):  
Thermophilic Fungus ◽  
Thermomyces Lanuginosus

Production, purification and characterization of thermomycolase, the extracellular serine protease of the thermophilic fungus Malbranchea pulchella var. sulfurea

1976 ◽  
Vol 22 (2) ◽  
pp. 165-176 ◽  
Author(s):  
Poh Seng Ong ◽  
G. Maurice Gaucher
Keyword(s):  
Serine Protease ◽  
Thermophilic Fungus ◽  
Amino Acid Residues ◽  
Submerged Cultures ◽  
Ph Optimum ◽  
Alkaline Serine Protease ◽  
Associated Production ◽  
Specificity Study ◽  
Malbranchea Pulchella ◽  
The Stability

The thermophilic fungus Malbranchea pulchella produces a single extracellular, alkaline, serine protease when grown at 45 °C, on 2% casein as sole carbon source. The growth-associated production of protease in submerged cultures was inhibited by addition of glucose, amino acids, or yeast extract. A simple four-step purification which yields homogeneous protease in 78% yield is described. The protease has an isoelectric point of 6.0, a pH optimum of 8.5, and is completely inhibited by serine protease inhibitors. A specificity study with small synthetic ester substrates indicated that the protease preferentially hydrolyzed bonds situated on the carboxyl side of aromatic or apolar amino acid residues which are not β-branched, positively charged or of the D configuration. Peptidase substrates and others such as N-acetyl-L-tyrosine-ethyl ester were not hydrolyzed. The protease was stable over a broad range of pH (6.5–9.5 at 30 °C, 20 h), and was particularly thermostable (t1/2 = 110 min at 73 °C, pH 7.4) in the presence of Ca2+ (10 mM). Macromolecules and Ca2+ also provide protection against the significant autolysis which occurs at pure protease concentrations greater than 0.01 mg/ml, as well as against surface denaturation which is enhanced by the presence of a silicone antifoam agent. Hence the stability of protease in submerged cultures is rationalized.

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