Biotechnology and Food Science

Stały URI zbioruhttp://hdl.handle.net/11652/3940

Biotechnology and Food Science publikuje artykuły oryginalne i przeglądowe dotyczące wszystkich aspektów biotechnologii i żywności oraz dziedzin pokrewnych.Czasopismo jest miejscem wymiany informacji w następujących dziedzinach:biotechnologia, chemia, technologia i toksykologia żywności, chemia i biotechnologia środowiska, chemia nieorganiczna, organiczna i fizyczna, biochemia, enzymologia, mikrobiologia, chemia medyczna, inżynieria chemiczna korozja mikrobiologiczna. Biotechnology and Food Science jest czasopismem ogólnie dostępnym, ukazuje się dwa razy w roku w wersji drukowanej i on-line. Pełne teksty artykułów są dostępne (www.bfs.p.lodz.pl). Wszystkie prace są recenzowane i oceniane pod względem jakości i oryginalności.



Czasopismo wydawane jest od 1955 roku, najpierw jako Zeszyty Naukowe Politechniki Łódzkiej. Chemia Spożywcza (1955-1979), następnie jako Zeszyty Naukowe Politechniki Łódzkiej. Technologia i Chemia Spożywcza (1980-1997) i Zeszyty Naukowe Politechniki Łódzkiej. Chemia Spożywcza i Biotechnologia (1998-2010).



ISSN 2299-6818 Częstotliwość wydawania: półrocznik (wersja drukowana i online) Wersja pierwotna: druk Język: angielski

Redaktor naczelny: Małgorzata Piotrowska tel: +48 42-631-34-70, e-mail: malgorzata.piotrowska@p.lodz.pl Adres redakcji: Wydział Biotechnologii i Nauk o Żywności Politechniki Łódzkiej Stefanowskiego 4/10, 90-924 Łódź tel.: 42-631-34-10, 42-636-28-60 fax: +48 42-636-28-60 e-mail: bfs@info.p.lodz.pl Wydawca: Wydawnictwo Politechniki Łódzkiej Wólczańska 223, 90-924 Łódź phone/fax: +48 42 631 29 52 www.wydawnictwa.p.lodz.pl

DOI: https://doi.org/10.34658/bfs/ Punkty MNiSW 2019: 5

Indeksacja: BazTech Agro Index Copernicus - ICI Journals Master List Dziedziny: rolnictwo, biotechnologia i mikrobiologia stosowana, chemia, nauka i technologia żywności

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  • Pozycja
    Production of co-immobilized dextransucrase and dextranase preparations and their application in isomalto-oligosaccharides synthesis
    (Wydawnictwo Politechniki Łódzkiej, 2017) Sikora, Barbara; Kubik, Celina; Bielecki, Stanisław
    Dextransucrase (DS) from Leuconostoc mesenteroides and dextranase (DN) from Penicillium funiculosum were co-immobilized by entrapment in calcium alginate and used to produce isomaltooligosaccharides (IMOs) from sucrose. DS convert sucrose into dextran, which is the substrate for DN, so that IMOs are products of dextran hydrolysis. Before the co-immobilization DS was cross-linked with glutardialdehyde (GA), while DN was adsorbed on hydroxyapatite (HAp). Cross-linking was essential for the stability of DS and pre-immobilization of DN to prevent enzyme from leaking out of the alginate beads. Operational stability of co-immobilized preparations of DS and DN was estimated based on amounts of isomaltose and isomaltotriose formed during successive 24h processes of IMOs synthesis, carried out at 30oC, pH 5.4 and 200 rpm in 10% (w/v) sucrose solutions. Preparation characterized by the initial DS/DN activities ratio of 1/14 was found to maintain these activities at least 100 h of IMOs synthesis (5 repeated batch reaction).
  • Pozycja
    A comparison of two enzymatic methods of clinical dextran production
    (Wydawnictwo Politechniki Łódzkiej, 2017) Sikora, Barbara; Kubik, Celina; Bielecki, Stanisław
    The aim of this study was to evaluate and compare of the two enzymatic methods of clinical dextran production were compared. The reactions were performed at 30°C and pH 5.4 in solutions containing different amounts of sucrose, using dextransucrase (DS, in the presence of dextranase (D) (method 1) or acceptor dextrans (method 2). The activity of Leuconostoc mesenteroides L dextransucrase (DS), which converts sucrose to dextran, was 0.4 U ml-1 in both the methods. As much as 53-56% of clinical dextran fractions were obtained for 28 h from 10% sucrose solutions, which contained 1.5% or 2.5% acceptor dextrans with molecular mass of 10 and 15 kDa, respectively. Approximately 50% of these fractions was obtained (also in 28 h) from 10% sucrose solutions by using 0.004 U ml-1 of DN, added to reaction mixtures 5 h later than Our experiments indicate that the clinical dextran can be efficiently produced by using both the compared methods, which employ either acceptor dextrans with definite molecular mass, or the dextranase. Because consumption of the latter enzyme is rather small, and it is easily available, thus this method should be attractive for clinical dextran manufacturers.
  • Pozycja
    Laccases – enzymes with an unlimited potential
    (Lodz University of Technology Press, 2017) Szczęsna-Antczak, Mirosława; Benedykt Kaczmarek, Michał; Kwiatos, Natalia; Bielecki, Stanisław
    Laccases (EC 1.10.3.2) are among the few enzymes, the history of which dates back to the 19th century. These oxidoreductases are present in almost all known fungi, some species of higher plants and insects. Moreover, in recent years, these enzymes have also been found in some bacterial organisms. Due to their significant properties and structure of the catalytic centre, laccases have been classified as the multicopper oxidases (MCOs). These enzymes are able to catalyse the oxidation of phenolic and non-phenolic compounds, with the aid of small molecules referred to as mediators. Thanks to their diverse nature, laccases have gained attention of both scientists and entrepreneurs from all over the world. Their significance is reflected in countless scientific and industrial applications, wherein laccases have become inseparable from chemical syntheses, the food industry, textile industry, biosensor design and the environmental protection. This paper gathers the most important information and the latest scientific discoveries relating to this desirable biocatalyst.