Studies on the Production of Milk-clotting Enzymes, Proteolytic Enzymes and Mucilage by Fungi

Abdelfattah, Ahmed; El-Hawwary, Nadia M.; Amr, Ali S.

doi:10.1099/00221287-84-2-327

Cited by 11 publications

(3 citation statements)

References 3 publications

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“…The ratio of milk-clotting activity to general proteolytic activity for an enzyme preparation is an index of its suitability as a rennin substitute (Abel-Fattah and El-Hawwary, 1974). So, the ratio of milk-clotting activity to proteolytic activity of the purified enzyme was estimated and compared with those of some commercial milk coagulating enzymes (Table 4).…”

Section: Milk Coagulationmentioning

confidence: 99%

Ginger rhizome as a potential source of milk coagulating cysteine protease

et al. 2011

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Section: Milk Coagulationmentioning

confidence: 99%

Ginger rhizome as a potential source of milk coagulating cysteine protease

et al. 2011

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“…Several researchers have confirmed superiority of curdling potential of the rennet produced by SSF to that produced by SF, with several fungal microorganisms being tested [34,35]. On the other hand there are studies which reported lower proteolytic potential for the rennet produced through SSF than the rennet produced through SF and from the same origin [36,37]. This could mean that SSF is a better choice for milk-coagulating enzymes used in cheese production industry.…”

Section: Resultsmentioning

confidence: 96%

Optimization of Fungal Rennet Production by local isolate of Rhizomucor nainitalensis Under Solid Substrate Fermentation system

Khademi¹

2013

IOSR-JPBS

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In this study the production of substitute rennet by a newly isolated thermophilic fungus, Rhizomucor nainitalensis, using optimized solid substrate fermentation system have been explored. The results revealed that enzyme activity is at its highest level at 40˚C, 50 % humidity, inoculation volume of 10 3 spore /gr wheat bran, and exoenzyme biosynthesis induction by casein at a rate of 1.5 %. Enzyme activity reached its highest (8400 SU/gr wheat bran) after 110 hours of incubation under the stated conditions. Precipitated enzyme, by addition of ammonium sulfate with milk coagulating activity of 115000 SU/gr enzyme powder, was free of toxin and microorganisms, with market's favorable aroma.

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“…The ratio of milk-clotting activity to general proteolytic activity to prepare an enzyme is its suitability index as a rennin milk substitute [36,37]. So the ratio of milk-clotting activity to proteolytic activity of the puriWed enzyme was estimated and compared with those of some commercial milk-coagulating enzymes (Table 3).…”

Section: Milk-clotting and Coagulation Activitymentioning

confidence: 99%

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Nadaroğlu

Demir

2012

Eur Food Res Technol

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In this research, a protease from the compositae (Scorzonera hispanica L.) was extracted and puriWed through (NH 4 ) 2 SO 4 precipitation, CM-Sephadex and Sephacryl S200. At the end of puriWcation by gel Wltration on a Sephacryl S-200 column, 87.11-fold puriWcation was achieved. It was shown that puriWed enzyme was homogeneous in terms of SDS-PAGE with molecular mass estimate of 30 kDa. The enzyme named compositain depicted an optimal pH of 8.0 and was stable at pH 7.0-9.0, and its optimal temperature was at 50°C. While Tween 80 (0.2 %) was activated to the puriWed protease enzyme, it was partially inhibited by 5 mM concentration of some metal salts and EDTA, PMSF, dithiothreitol, H 2 O 2 and -mercaptoethanol. The enzyme activity was stable even in the presence of detergents and organic solvents. In addition, it was investigated whether the puriWed and characterized protease enzyme would cause to congeal milk. As a result, it was determined that the compositain could congeal milk and it would be used for cheese production. The compositain had potential application in food processing.

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Studies on the Production of Milk-clotting Enzymes, Proteolytic Enzymes and Mucilage by Fungi

Cited by 11 publications

References 3 publications

Ginger rhizome as a potential source of milk coagulating cysteine protease

Ginger rhizome as a potential source of milk coagulating cysteine protease

Optimization of Fungal Rennet Production by local isolate of Rhizomucor nainitalensis Under Solid Substrate Fermentation system

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

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