funalia trogii
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2020 ◽  
Vol 215 ◽  
pp. 05003
Author(s):  
Sergei Sorokin ◽  
Mark Shamtsyan ◽  
Nicolai Petrishchev

Currently, the search continues for fibrinolytic and thrombolytic drugs that quickly dissolve blood clots and do not have side effects. One of the directions of these studies is the production of fibrinolytic enzymes from deep cultures of basidiomycetes. This work examines the fibrinolytic activity of culture liquids obtained from two cultures of saprophytic basidiomycetes: Coprinus lagopides and Funalia trogii in comparison with the commercial thrombolytic drug Actilyse.


2020 ◽  
Vol 215 ◽  
pp. 01006
Author(s):  
Artem Khludin ◽  
Boris Kolesnikov ◽  
Nikita Khrapatov ◽  
Mark Shamtsyan

Hydrophobins are low-molecular surface-active proteins of fungi with high surface activity and the ability to self-assemble at the interface. The unusual properties of hydrophobins open up possibilities for their application in various fields, including medicine and the food industry. The wide range of possible applications of hydrophobins makes it important to develop and improve technology for their isolation and purification. The aim of the study was to select methods for the extraction of hydrophobin-type proteins and to study the ability of the obtained extracts to modify the solid surface. The source of hydrophobins in this study was the biomass of the fungus Funalia trogii. Methods for the isolation of hydrophobin-type proteins were developed, including purification of the extract from ballast proteins, followed by the destruction of agglomerates of hydrophobin-type proteins using acids in high concentrations. The surface activity and the ability to modify the surface of the obtained proteins were evaluated. As a result, we obtained extracts containing hydrophobin-type proteins with high surface activity. Funalia trogii extracts are capable of changing the hydrophobicity of the surface and can be used in various industries.


Processes ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 36 ◽  
Author(s):  
Sanaz Khalighi ◽  
Ralf G. Berger ◽  
Franziska Ersoy

The native extractable arabinoxylans (AX) from wheat bran were cross-linked by the commercial laccase C (LccC) and self-produced laccases from Funalia trogii (LccFtr) and Pleurotus pulmonarius (LccPpu) (0.04 U/µg FA, each). Dynamic oscillation measurements of the 6% AX gels demonstrated a storage modulus of 9.4 kPa for LccC, 9.8 kPa for LccFtr, and 10.0 kPa for LccPpu. A loss factor ≤ 0.6 was recorded in the range from 20 to 80 Hz for all three laccases, and remained constant for four weeks of storage, when LccFtr and LccPpu were used. Arabinoxylan gel characteristics, including high water holding capacity, swelling ratio in saliva, and heat resistance indicated a covalently cross-linked network. Neither the mediator compounds caffeic acid and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid (ABTS), nor citrus pectin, enhanced the elastic properties of the gels. Using laccases as an oxidant provided gels with a solid and stable texture, comparable in firmness to traditional gelatin gels. Thus, AX gels can be presented in the vegan, halal, and kosher food markets. They may also find use in pharmaceutical and other industrial applications.


Processes ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 16 ◽  
Author(s):  
Sanaz Khalighi ◽  
Ralf G. Berger ◽  
Franziska Ersoy

Sugar beet fibre (fibrex) is an abundant side-stream from the sugar refining industry. A self-produced laccase from Funalia trogii (LccFtr) (0.05 U/µg FA) successfully cross-linked fibrex to an edible gel. Dynamic oscillation measurements of the 10% fibrex gels showed a storage modulus of 5.52 kPa and loss factors ≤ 0.36 in the range from 20 to 80 Hz. Comparing storage stability of sweetened 10% fibrex gels with sweetened commercial 6% gelatin gels (10% and 30% d-sucrose) indicated a constant storage modulus and loss factors ≤ 0.7 during four weeks of storage in fibrex gels. Loss factors of sweetened gelatin gels were ≤0.2, and their storage modulus decreased from 9 to 7 kPa after adding d-sucrose and remained steady for four weeks of storage. Fibrex gel characteristics, including high water holding capacity, swelling ratio in saliva, and heat resistance are attributed to a covalently cross-linked network. Vanillin, as a mediator, and citrus pectin did not enhance covalent cross-links and elastic properties of the fibrex gels. Thus, laccase as an oxidative agent provided gels with a solid and stable texture. Fibrex gels may find uses in pharmaceutical and other industrial applications, which require a heat-resistant gel that forms easily at room temperature. They also represent an ethical alternative for manufacturing vegan, halal, and kosher food.


2019 ◽  
Vol 55 (6) ◽  
pp. 1067-1068
Author(s):  
Jian-Hai Ding ◽  
Zheng-Hui Li ◽  
Tao Feng ◽  
Ji-Kai Liu
Keyword(s):  

2018 ◽  
Vol 20 (7) ◽  
pp. 657-664 ◽  
Author(s):  
Ivan V. Zmitrovich ◽  
Margarita A. Bondartseva ◽  
Stanislav P. Arefyev ◽  
Oleg N. Ezhov ◽  
Solomon P. Wasser
Keyword(s):  

2017 ◽  
Vol 45 (2) ◽  
pp. 89-101 ◽  
Author(s):  
Julia Kolwek ◽  
Christoph Behrens ◽  
Diana Linke ◽  
Ulrich Krings ◽  
Ralf G. Berger
Keyword(s):  
One Pot ◽  

2017 ◽  
Vol 72 (5-6) ◽  
pp. 173-179 ◽  
Author(s):  
Y. Doruk Aracagök ◽  
Hakan Göker ◽  
Nilüfer Cihangir

Abstract Pharmaceuticals are widely used for treating human and animal diseases. Naproxen [(S) 6-methoxy-α-methyl-2-naphthalene acetic acid] and its sodium salt are members of the α-arylpropionic acid group of nonsteroidal anti-inflammatory drugs. Due to excessive usage of naproxen, this drug has been determined even in drinking water. In this study, four fungal strains Phanerochaete chrysosporium, Funalia trogii, Aspergillus niger, and Yarrowia lipolytica were investigated in terms of naproxen removal abilities. According to LC/MS data, A. niger was found the most efficient strain with 98% removal rate. Two main by-products of fungal transformation, O-desmethylnaproxen and 7-hydroxynaproxen, were identified by using LC/MS, 1HNMR, and 13CNMR. Our results showed that O-demethylation and hydroxylation of naproxen is catalyzed by cytochrome P450 enzyme system.


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