Mold Metabolites. II. The Structure of Sorbicillin, a Pigment Produced by the Mold Penicillium notatum

1948 ◽  
Vol 70 (12) ◽  
pp. 4240-4243 ◽  
Author(s):  
Donald J. Cram
Keyword(s):  
Penicillium Notatum

SUR DES ANTIGENES DU PENICILLIUM NOTATUM

Allergy ◽  
1948 ◽  
Vol 1 (4) ◽  
pp. 297-310 ◽  
Author(s):  
H. ISLER ◽  
A. KARABADJAKIAN
Keyword(s):  
Penicillium Notatum

Thermal stability of ribosomes from a thermophilic and a mesophilic fungus

1973 ◽  
Vol 19 (6) ◽  
pp. 761-763 ◽  
Author(s):  
H. M. Miller ◽  
M. G. Shepherd
Keyword(s):  
Thermal Stability ◽  
Ion Concentration ◽  
Magnesium Ion ◽  
Penicillium Notatum ◽  
Ribosomal Subunits ◽  
Ion Concentrations ◽  
Thermal Stability Of

Ribosomes and ribosomal subunits from the thermophile Penicillium duponti were found to be more thermostable than the corresponding particles from the mesophile Penicillium notatum. The thermostability of the ribosomes from both organisms was dependent on magnesium ion concentration. The dissociation of the 80-S ribosomes into 60-S and 40-S subunits occurred at higher magnesium ion concentrations for the mesophile than the thermophile.

Production and Thermal Characterization of an Alkaline Pectin Lyase from Penicillium notatum

2015 ◽  
Vol 11 (4) ◽  
pp. 517-525 ◽  
Author(s):  
Umme Habibah Siddiqua ◽  
Haq Nawaz Bhatti ◽  
Shazia Nouren ◽  
Saima Noreen ◽  
Ismat Bibi
Keyword(s):  
Ammonium Sulphate ◽  
Thermal Inactivation ◽  
Thermal Characterization ◽  
Maximal Activity ◽  
Inhibitory Effect ◽  
Pectin Lyase ◽  
Partial Purification ◽  
Penicillium Notatum ◽  
Enhanced Production ◽  
Lyase Activity

Abstract The present study was aimed to investigate the potential of Penicillium notatum for the production of pectin lyase under solid state culture using wheat bran as substrate. Different process parameters were optimized using completely randomized design for enhanced production of the pectin lyase. P. notatum showed maximum production (1875 U/gds) of pectin lyase with substrate amount 15 g/250 ml, moisture level 60%, pH 6, incubation period 120 h at 30°C. Pectin lyase activity was further improved with the addition of maltose and ammonium sulphate as carbon and nitrogen additives (1%), respectively. Partial purification of enzyme was carried out by ammonium sulphate precipitation at 80% saturation level. The P. notatum pectin lyase showed maximal activity at 65°C and pH 8. Km and Vmax values were 0.29% and 0.487 µmol/min, respectively. Energy of activation was found to be 5.33 kJ/mol. A detailed kinetic study of thermal inactivation was carried out. The results showed that pectin lyase exhibited resistance against thermal unfolding. Effect of various metals on pectin lyase activity was also investigated. All the metals showed inhibitory effect on the enzyme activity. The present investigation revealed that pectin lyase isolated from P. notatum is thermally stable and alkaline in nature.

scholarly journals Sensitisation to Aspergillus Fumigatus and Penicillium Notatum in Laboratory Workers

1999 ◽  
Vol 12 (1) ◽  
pp. 205873929901200 ◽  
Author(s):  
P. Boscolo ◽  
R. Piccolomini ◽  
F. Benvenuti ◽  
G. Catamo ◽  
M. Di Gioacchino
Keyword(s):  
Aspergillus Fumigatus ◽  
Penicillium Notatum ◽  
Laboratory Workers
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