scholarly journals Enhanced Performance of Immobilized Rhizopus oryzae Lipase on Coated Porous Polypropylene Support with Additives

Catalysts ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 303
Author(s):  
Fatimah Sani ◽  
Nur Fathiah Mokhtar ◽  
Mohd Shukuri Mohamad Ali ◽  
Raja Noor Zaliha Raja Abd Rahman

The immobilization of Rhizopus oryzae lipase (RoL) by hydrophobic adsorption on polypropylene supports with additives was investigated. Additives such as hen egg albumin, sodium caseinate and CAVAMAX® W6 were used to coat the support during immobilization where the immobilized RoL on coated support was compared to those of noncoated support. Following the immobilization, the catalytic activity of immobilized RoL was characterized based on different temperatures and pH. The immobilized RoL without additives showed optimal lipase activity at an optimum temperature of 50 °C and pH 6. However, RoL lipase that was immobilized on support treated with CAVAMAX® W6 had better performance in terms of hydrolytic activity and stability as compared to other additives. In addition, by having a support treated with hen egg albumin, the immobilized RoL was capable of yielding higher ester during esterification reactions.

2001 ◽  
Vol 86 (1) ◽  
pp. 59-70 ◽  
Author(s):  
Stefan Minning ◽  
Alicia Serrano ◽  
Pau Ferrer ◽  
Carles Solá ◽  
Rolf D. Schmid ◽  
...  

2007 ◽  
Vol 6 (1) ◽  
pp. 21 ◽  
Author(s):  
David Resina ◽  
Mónika Bollók ◽  
Narendar K Khatri ◽  
Francisco Valero ◽  
Peter Neubauer ◽  
...  

2001 ◽  
Vol 31 (5) ◽  
pp. 839-842 ◽  
Author(s):  
Clóvis de Paula Santos ◽  
Terezinha Padilha ◽  
Maria de Lurdes de Azevedo Rodrigues

The effect of different temperatures on the predatory activity of Arthrobotrys oligospora and Duddingtonia flagrans on the free-living larval stages of cyathostomes were evaluated in an experiment where feces of horses containing the parasites’ eggs were treated with these fungi and incubated under different constant temperatures (10°C, 15°C, 20°C, 25°C and 30°C ). The results indicated that the optimum temperature for egg development was 25°C. At 10°C the number of L3 recovered was practically zero, and at 15°C and 20°C, the percentage of larvae recovered was less than 3% of the total number of eggs per gram of feces. When these cultures subsequently were incubated for an additional period of 14 days at 27°C, they allowed the development of L3. In all the cultures inoculated with fungi a significant reduction in the number of larvae was observed. When incubated at 25°C or 30°C, the fungi caused reductions above 90%, in the number of L3. The samples cultivated at 10°C, 15°C, 20°C, 25°C and 30°C, when incubated for an additional period of 14 days at 27°C the reduction percentage of larvae was above 90% for A. oligospora. However, the same did not occur for D. flagrans. Here a reduction percentage between 47.5% and 41.8% was recorded when the cultures were incubated at 10°C and 20°C, respectively. The two species of fungi tested showed to be efficient in reducing the number of L3 when mixed with equine feces and maintained at the same temperature for the development of larval pre-parasitic stages of cyathostomes.


1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.


2006 ◽  
pp. 48-57
Author(s):  
R. C. Ray

The study was conducted to determine the production in vitro and in vivo of cellulases by Botrydiplodia theobromae and Rhizopus oryzae. Isolates of these organisms were obtained from the postharvest decay of sweetpotato tubers. Results revealed that B. theobrornae and R. oryzae which were isolated from postharvest spoilage of sweetpotato tubers produced endo-13-1,4-glucanase and exo-V-1 ,4-glucanase in culture and in fungi-infected tissues of sweetpotato tubers. The optimum temperature and pH for cellulose synthesis and activity were 30°C and pH 6.5, respectively.


1929 ◽  
Vol 6 (3) ◽  
pp. 275-292
Author(s):  
N. J. BERRILL

1. The mechanism of feeding and digestion in the Pyurid Ascidians Tethyum pyriforme americanum and Boltenia ovifera is described. 2. The structure and histology of the "liver" is described and it is shown that it is primarily an organ of secretion. 3. It is found that the only digestive enzymes are those poured into the gut by the liver, and consist of a powerful amylase, a protease, a very weak lipase, and also an invertase, a maltase, and a lactase. 4. The brownish pigment of the liver gives reactions with acids somewhat like those of bile pigment. There is no trace of bile salts, however, nor of cholesterol. 5. The amylase has an activity range from pH 6.0 topic pH 8.5 with an optimum near pH 7.5. The protease is active from pH 6.0 to above pH 10.0. A similar protease is secreted by Molgula citrina and Ascidia prunum. 6. The relative strengths of the amylase and protease are compared, the amylase being very much the stronger. 7. While experiments of brief duration indicate an optimum temperature for enzyme activity above 40° C, the more prolonged the experiments the lower does the optimum become. Whatever the optimum may be after an experiment of 2 hours' duration, it falls about 20° C. during the next 45 hours, if the experiments be so prolonged. 8. At 15° C. and at 10° C. the food takes about 35 and 55 hours respectively to pass through the alimentary canal, and at 50 C. somewhere between 70 and 90 hours. These temperatures approximately cover the normal range in temperature of the environment, and therefore of the animal itself. 9. From experiments lasting 33 hours the optimum temperature for enzyme activity was found to be about 17° C.; that is, within one or two degrees of the body temperature. From experiments lasting 57 hours the optimum temperature was found to be about 13° C ; that is, within three degrees of the body temperature. 10. These temperature optima not only represent the relative amounts of substrate converted at different temperatures, but also represent the absolute amounts converted and convertible. 11. The enzymes, amylase and protease, are two-thirds to three-quarters destroyed during their period of activity within the alimentary canal of the animal, and in order to utilise the remainder the digestion mixture would have to be retained within the canal for twice as long a time. 12. Therefore it seems probable that the organism in making such a compromise between a high activity of the enzyme and its economical use is working to a maximum efficiency; and it is possible that a permanent increase in the stability of the digestive enzymes would be turned to advantage through a more prolonged retention of the food within the gut.


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