SECRETION OF A GLUCOSE OXIDIZING ENZYME WITH BACTERIOSTATIC PROPERTY BY PENICILLIUM NOTATUM

1944 ◽  
Vol 124 (13) ◽  
pp. 924 ◽  
Allergy ◽  
1948 ◽  
Vol 1 (4) ◽  
pp. 297-310 ◽  
Author(s):  
H. ISLER ◽  
A. KARABADJAKIAN
Keyword(s):  

1973 ◽  
Vol 19 (6) ◽  
pp. 761-763 ◽  
Author(s):  
H. M. Miller ◽  
M. G. Shepherd

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.


2015 ◽  
Vol 11 (4) ◽  
pp. 517-525 ◽  
Author(s):  
Umme Habibah Siddiqua ◽  
Haq Nawaz Bhatti ◽  
Shazia Nouren ◽  
Saima Noreen ◽  
Ismat Bibi

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.


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