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Thermal inactivation of native and crosslinked invertases
Date
1997-09-01
Author
Kaplan, O
Bakir, U
Erarslan, A
Metadata
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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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Formaldehyde and three homobifunctional bisimidoesters having different lengths, dimethyl suberimidate (DMS), dimethyl adipimidate (DMA), dimethyl-3,3'-dithiobispropionimidate (DTBP), were used to crosslink invertase. Optimal concentrations for crosslinking with DMS and formaldehyde were determined as 0.3% and 0.015%, respectively. Inactivation mechanisms of the native, DMS and formaldehyde cross-linked invertases were first order during prolonged heat treatment. The maximum stabilization factors with DMS and formaldehyde were 1.5 at 55 degrees C and 1.7 at 57.5 degrees C, respectively. V-max and K-m values decreased 5 to 10% by DMS and formaldehyde crosslinking. On the other hand, crosslinking with DMA and DTBP decreased stability against inactivation.
Subject Keywords
Escherichia-coli atcc-11105
,
Cross-linking
,
Yeast invertase
,
Identification
,
Stabilization
,
Residue
,
Mutant
URI
https://hdl.handle.net/11511/67232
Journal
BIOTECHNOLOGY TECHNIQUES
Collections
Department of Food Engineering, Article
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O. Kaplan, U. Bakir, and A. Erarslan, “Thermal inactivation of native and crosslinked invertases,”
BIOTECHNOLOGY TECHNIQUES
, pp. 621–623, 1997, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/67232.