Results 211 to 220 of about 9,989 (259)
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Crystal Structure of The Rhizomucor miehei Aspartic Proteinase

1998
The composition of milk has been reviewed by Jenness (1). It is an extremely complex mixture of components, consisting of water, lipids, carbohydrates, proteins, salts and many miscellaneous compounds. The largest component is water. The lipids are 98% triglycerides, mostly as globules. Carbohydrate is mainly as lactose.
J W, Quail   +3 more
openaire   +2 more sources

Immobilization of Rhizomucor miehei lipase onto the organic functionalized SBA-15: Their enzymatic properties and glycerolysis efficiencies for diacylglycerols production.

Food Chemistry, 2019
In this study, mesoporous silica SBA-15 was modified by organic functional groups through silanization. Series of organosilane compounds were grafted onto the SBA-15, and the obtained functionalized carriers were then used to immobilize the lipase from ...
Nanjing Zhong   +3 more
semanticscholar   +1 more source

Rhizomucor tauricus: a questionable species of the genus

Mycological Research, 1999
To test the validity of R. tauricus as a separate species, its carbon source utilization, isoenzyme patterns and PCR-coupled RFLP of the ITS of its rDNA were analysed. Whilst R. tauricus differed considerably from R. pusillus and R. miehei in morphological traits as well as its ability to row on single carbon sources, the results obtained from all ...
Csaba Vágvölgyi   +2 more
openaire   +1 more source

High stabilization of immobilized Rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers: Poly-allylamine/Aldehyde–dextran

, 2020
Immobilized enzymes have a very large surface region which is not in contact with the support surface and, thus, have potential as a target for novel stabilization strategies.
J. Cejudo-Sanches   +7 more
semanticscholar   +1 more source

Rhizomucor miehei lipase-catalysed synthesis of cocoa butter equivalent from palm mid-fraction and stearic acid: Characteristics and feasibility as cocoa butter alternative.

Food Chemistry, 2020
In this study, cocoa butter equivalents (CBEs) were prepared through enzymatic interesterification of palm mid-fraction (PMF) with stearic acid (SA). The reaction process parameters were experimented and the performance of the product was analysed.
Zhaoxian Huang   +7 more
semanticscholar   +1 more source

Optimisation of n-octyl oleate enzymatic synthesis over Rhizomucor miehei lipase

Bioprocess and Biosystems Engineering, 2006
Octyl oleate is a useful organic compound with several applications in cosmetic, lubricant and pharmaceutical industry. At first, the enzymatic synthesis of n-octyl oleate by direct lipase-catalysed esterification of oleic acid and 1-octanol was investigated in a stirred batch reactor in solvent-free system.
LAUDANI C. G   +5 more
openaire   +3 more sources

Early Starch Catabolism by Rhizomucor Pusillus

Mycologia, 1986
(1986). Early Starch Catabolism by Rhizomucor Pusillus. Mycologia: Vol. 78, No. 1, pp. 129-131.
P. R. Adams, J. J. Deploey
openaire   +1 more source

Rhizomucor miehei triglyceride lipase is synthesized as a precursor

Lipids, 1988
AbstractARhizomucor miehie cDNA library constructed inEscherichia coli was screened with synthetic oligonucleotides designed from knowledge of a partial amino acid sequence of the secreted triglyceride lipase (triacyl‐glycerol acylhydrolase EC 3.1.1.3) from this fungus. Lipase‐specific recombinants were isolated and their insert sequenced.
E, Boel   +4 more
openaire   +2 more sources

First case of fatal Rhizomucor miehei endocarditis in an immunocompromised patient.

Diagnostic microbiology and infectious disease, 2020
Rhizomucor miehei is a cause of bovine mycotic abortion and mastitis and has rarely been described in human disease. Here, we report the first isolation of R.
J. Hagemann   +6 more
semanticscholar   +1 more source

Rhizomucor miehei Aspartic Proteinases Having Improved Properties

1998
Aspartic proteinases are widely spread in most organisms, where they carry out many different functions. The oldest and most well–known use of aspartic proteinases is as coagulants in cheese–making. The coagulants are probably still the only commercial products containing aspartic proteinases as the active substance.
openaire   +2 more sources

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