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Fatma Işık Üstok

Researcher at University of Cambridge

Publications -  17
Citations -  332

Fatma Işık Üstok is an academic researcher from University of Cambridge. The author has contributed to research in topics: Bacillus megaterium & Spore germination. The author has an hindex of 10, co-authored 16 publications receiving 313 citations. Previous affiliations of Fatma Işık Üstok include İzmir Institute of Technology.

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Journal ArticleDOI

Solid-state production of polygalacturonase by Aspergillus sojae ATCC 20235

TL;DR: Solid-state fermentation provided 48% more polygalacturonase activity compared to submerged fermentation under individually optimized conditions.
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Biochemical and thermal properties of β-galactosidase enzymes produced by artisanal yoghurt cultures

TL;DR: β-Galactosidases produced by pure and mixed cultures of Streptococcus thermophilus 95/2 and Lactobacillus delbrueckii ssp bulgaricus 77 (Lb 77) isolated from the Toros mountain region of Turkey were characterised with respect to their biochemical and thermal properties and could be considered as potential candidates for lactose hydrolysis of milk and milk products.
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Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination.

TL;DR: In this study, in vitro and in vivo analyses have been used to clarify the roles of individual SleB and YpeB domains in PG degradation and support the role of this invariant glutamate as the key catalytic residue insleB and CwlJ.
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Optimization of the associative growth of novel yoghurt cultures in the production of biomass, β-galactosidase and lactic acid using response surface methodology

TL;DR: In this paper, the associative growth of Streptococcus thermophilus 95/2 and Lactobacillus delbrueckii ssp. bulgaricus 77 (Lb 77) isolated from the Toros mountain region of Turkey was investigated with respect to lactic acid, biomass and β-galactosidase enzyme production using response surface methodology (RSM).
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Mutational analysis of Bacillus megaterium QM B1551 cortex-lytic enzymes.

TL;DR: Data indicate that while the presence of either the N- or C-terminal domain of B. megaterium SleB is sufficient for initiation of cortex hydrolysis and the generation of anhydromuropeptides, the perceived lytic transglycosylase activity may be derived from an enzyme(s), perhaps exclusively or in addition to SleB, which has yet to be identified.