Fiber-structured cheese making with Irpex lacteus milk-clotting enzyme.
نویسندگان
چکیده
منابع مشابه
Biodegradation of 2,4,6-Trinitrotoluene by White-Rot Fungus Irpex lacteus
White-rot fungus Irpex lacteus degraded TNT significantly in proportion to the culture time. After 48 h incubation, about 95% of TNT was degraded. Two reduced metabolites were identified as 4-amino-2,6-dinitrotoluene (4-ADNT) and 2-amino-4,6-dinitrotoluene (2-ADNT) which was further degraded.
متن کاملPurification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei
Milk clotting enzyme (M CE) produced by: Rhizomucor miehei was purified and characterized.The enzyme was purified 220.29-fold with specific activity about 14444.2 U/mg protein byultrafiltration, ammonium sulfate fractionation, Sephacryl S-300 chromatography. The maximumenzyme activity was at 65°C.The milk clotting activity was decreased steadily as pH is increased and indicated maximumactivity ...
متن کاملThe promoting effect of byproducts from Irpex lacteus on subsequent enzymatic hydrolysis of bio-pretreated cornstalks
BACKGROUND Irpex lacteus, a versatile lignin-degrading fungus with various extracellular enzymes, has been widely used for biological pretreatment. However, most studies have focused on the change of substrate structure after biological pretreatment, and the effect of these changes on the enzymatic hydrolysis, but the effect of byproducts from biological pretreatment process on subsequent enzym...
متن کاملUtilization of salt whey from Egyptian Ras (cephalotyre) cheese in microbial milk clotting enzymes production.
BACKGROUND Microbial milk-clotting enzymes are valued as calf rennet substitutes in the cheese industry. The worldwide increase of cheese production coupled with a reduced supply of calf rennet has prompted a search for calf rennet substitutes, including microbial and plant rennets. However, most plant rennets have proved unsuitable because they impart a bitter taste to the cheese. Microbial re...
متن کاملExtra tyrosine in the carbohydrate-binding module of Irpex lacteus Xyn10B enhances its cellulose-binding ability.
The xylanase (Xyn10B) that strongly adsorbs on microcrystalline cellulose was isolated from Driselase. The Xyn10B contains a Carbohydrate-binding module family 1 (CBM1) (IrpCBMXyn10B) at N-terminus. The canonical essential aromatic residues required for cellulose binding were conserved in IrpCBMXyn10B; however, its adsorption ability was markedly higher than that typically observed for the CBM1...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1988
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.52.1277