scholarly journals Characterization of the gatA gene from Aspergillus oryzae

2016 ◽  
Vol 16 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Motoaki Sano ◽  
Mitsuko Dohmoto ◽  
Shinichi Ohashi
Keyword(s):  
2010 ◽  
Vol 62 (2) ◽  
pp. 557-564 ◽  
Author(s):  
Mayumi Matsushita-Morita ◽  
Sawaki Tada ◽  
Satoshi Suzuki ◽  
Ryota Hattori ◽  
Junichiro Marui ◽  
...  

2009 ◽  
Vol 86 (1) ◽  
pp. 213-226 ◽  
Author(s):  
Chiara Gasparetti ◽  
Greta Faccio ◽  
Mikko Arvas ◽  
Johanna Buchert ◽  
Markku Saloheimo ◽  
...  

2012 ◽  
Vol 47 (1) ◽  
pp. 18-25 ◽  
Author(s):  
Mouna Sahnoun ◽  
Samir Bejar ◽  
Aïda Sayari ◽  
Mohamed Ali Triki ◽  
Mouna Kriaa ◽  
...  

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Christabel Ndahebwa Muhonja ◽  
Gabriel Magoma ◽  
Mabel Imbuga ◽  
Huxley Mae Makonde

This study aimed at molecular and biochemical characterization of low-density polyethene (LDPE) degrading fungi and bacteria from Dandora dumpsite, Nairobi. Twenty bacterial and 10 fungal isolates were identified using 16S rDNA and 18S rDNA sequences for bacteria and fungi, respectively. The highest fungal degradation was attributed to Aspergillus oryzae strain A5,1 while the highest bacterial degradation was attributed to Bacillus cereus strain A5,a and Brevibacillus borstelensis strain B2,2, respectively. Isolates were screened for their ability to produce extracellular laccase and esterase; Aspergillus fumigatus strain B2,2 exhibited the highest presence of laccase (15.67 mm) while Aspergillus oryzae strain A5,1 exhibited the highest presence of esterase (14.33 mm). Alkane hydroxylase-encoding genes were screened for using primer AlkB 1 which amplified the fragment of size 870 bp. Four bacterial samples were positive for the gene. Optimum growth temperature of the fungal isolates was 30°C. The possession of laccase, esterase, and alkane hydroxylase activities is suggested as key molecular basis for LDPE degrading capacity. Knowledge of optimum growth conditions will serve to better utilize microbes in the bioremediation of LDPE. The application of Aspergillus oryzae strain A5,1 and Bacillus cereus strain A5,a in polyethene degradation is a promising option in this kind of bioremediation as they exhibited significantly high levels of biodegradation. Further investigation of more alkane degrading genes in biodegrading microbes will inform the choice of the right microbial consortia for bioaugmentation strategies.


2017 ◽  
Vol 64 (3) ◽  
pp. 65-73 ◽  
Author(s):  
Akira Yoshimi ◽  
Misa Hirama ◽  
Yasunobu Tsubota ◽  
Kazuyoshi Kawakami ◽  
Silai Zhang ◽  
...  

2019 ◽  
Vol 21 (1) ◽  
pp. 297 ◽  
Author(s):  
Triinu Visnapuu ◽  
Aivar Meldre ◽  
Kristina Põšnograjeva ◽  
Katrin Viigand ◽  
Karin Ernits ◽  
...  

Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (Ki = 0.8 µM) and Tris (Ki = 70.5 µM). BaAG2 was competitively inhibited also by isomaltose-like sugars and a hydrolysis product—glucose. At high maltose concentrations, BaAG2 exhibited transglycosylating ability producing potentially prebiotic di- and trisaccharides. Atypically for yeast maltases, a low but clearly recordable exo-hydrolytic activity on amylose, amylopectin and glycogen was detected. Saccharomyces cerevisiae maltase MAL62, studied for comparison, had only minimal ability to hydrolyze these polymers, and its transglycosylating activity was about three times lower compared to BaAG2. Sequence identity of BaAG2 with other maltases was only moderate being the highest (51%) with the maltase MalT of Aspergillus oryzae.


Sign in / Sign up

Export Citation Format

Share Document