Induction and characterization of a novel amine oxidase from the yeast Kluyveromyces marxianus

Abstract

An amine oxidase from the yeast Kluyveromyces marxianus was induced, purified and completely characterized; it was shown to belong to the class of coppercontaining amine oxidases (E.C. 1.4.3.6). The enzyme was induced by putrescine and, very strongly, by copper(II); structural-functional characterization of the enzyme was performed, including determination of molecular weight, glycosylation, copper and TPQ content, isoelectric point, K M and k CAT (with benzylamine as substrate), pH, temperature and ionic strength effect on catalysis, substrate and inhibitor specificity. A 700 bp clone was isolated containing the cDNA that encodes for the C-terminus of the enzyme; the amino acid sequence deduced (the first available for a benzylamine oxidase from yeast) was compared to that of other copper amine oxidases from microorganisms and higher organisms. From the results obtained, the putrescine/benzylamine oxidase from Kluyveromyces marxianus was found to have a good homology with other enzymes of this class from microorganisms, and particularly with AO I from Aspergillus niger. Nonetheless, some features resulted closer to those of animal amine oxidases and histaminases. Some potential biotechnological applications are proposed. The cDNA Accession No. is AJ320485.

Enzymes for Wine Fermentation: Current and Perspective Applications

“…1.4.3.6). The latter have been detected in various yeasts such as Kluyeromyces marxianus or Debaryomyces hansenii [105,106]. These enzymes belong to the class of type 2 or "non-blue" copper proteins which convert primary amines to the corresponding aldehydes with an equimolar consumption of molecular oxygen and formation of hydrogen peroxide and ammonia.…”

The Potential of the Yeast Debaryomyces hansenii H525 to Degrade Biogenic Amines in Food

“…The majority of the proteins focused in the range of 4.5 to 5.2 (not shown). Corpillo et al [ 20 ] characterized an amine oxidase of the yeast Kluyveromyces marxianus with a similar pI of 3.9. Based on these data, the ampholyte solution for the pIEF was selected, which was in the acidic pH range (3–5).…”

Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes

“…‘Weakly accepted substrate’ (yellow) refers to an enzyme activity of less than 8% compared to the most favored substrate or if the activity/selectivity was described as “weak” in the respective literature. 1 (Sekiguchi et al 2004 ), 2 (Lee and Kim 2013a ), 3 (Choi et al 1995 ), 4 (Shimizu et al 1997 ), 5 (Sugawara et al 2014 ), 6 (Sugawara et al 2015 ), 7 (Schilling and Lerch 1995 ), 8 (Frébort et al 1996 ), 9 (Sadeghi et al 2020 ), 10 (Yamashita et al 1993 ), 11 (Corpillo et al 2003 ), 12 (Lee et al 2008 ), 13 (Kettner et al 2021 ), 14 (Šebela et al 1998 ), 15 (Schwelberger and Bodner 1997 ), 16 (Hill et al 1970 ) …”

“…If the HOX is also thought to be used for the degradation of other relevant biogenic amines, such as tyramine, cadaverine and putrescine, only the ‘amine oxidases’ from A. carbonarius AIU205, K. marxianus CBS5795 and A. niger AKU3302 as well as the DAO from Y. lipolytica PO1f would be suitable (Frébort et al 1996 ; Corpillo et al 2003 ; Sugawara et al 2015 ; Kettner et al 2021 ). Hereby, the ‘amine oxidase’ from K. marxianus CBS5795 and the DAO from Y. lipolytica PO1f showed the broadest substrate selectivity since they also deaminated spermidine oxidatively.…”