Production and characterization of a milk-clotting protease in the crude enzymatic extract from the newly isolated Thermomucor indicae-seudaticae N31

Autor:	Carolina Merheb-Dini, Roberto da Silva, Eleni Gomes, Maurício Boscolo
Rok vydání:	2010
Předmět:	Protease biology Chemistry medicine.medical_treatment food and beverages Rhizomucor miehei General Medicine biology.organism_classification Analytical Chemistry chemistry.chemical_compound Biochemistry Solid-state fermentation Casein medicine Fermentation Rennet Chymosin Pepstatin Food Science
Zdroj:	Food Chemistry. 120:87-93
ISSN:	0308-8146
DOI:	10.1016/j.foodchem.2009.09.075
Popis:	Microbial rennet-like milk-clotting enzymes are aspartic proteinases that catalyze milk coagulation, substituting calf rennet. Crude enzymatic extract produced by the thermophilic fungus, Thermomucor indicae-seudaticae N31, on solid state fermentation (SSF) using wheat bran, exhibited high milk-clotting activity and low proteolytic activity after 24 h of fermentation. Highest milk-clotting activity (MCA) was at pH 5.7, at 70 °C and in 0.04 M CaCl2; it was stable in the pH range 3.5–4.5 for 24 h and up to 45 °C for 1 h. MCA was highly inhibited by pepstatin A. Hydrolytic activity profile of the crude enzymatic extract on whole bovine casein, analyzed by gel electrophoresis (Urea–PAGE) and RP-HPLC revealed low proteolytic action towards casein fractions and a peptide profile similar to the one obtained with commercial Rhizomucor miehei protease (Hannilase).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::97b5af8107a69ab20257d5687ca39a8a https://doi.org/10.1016/j.foodchem.2009.09.075 Zobrazit plný text záznamu Full Text from ScienceDirect