Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification.

التفاصيل البيبلوغرافية
العنوان:	Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification.
المؤلفون:	Halalipour A; Department of Food Science and Technology, University of Georgia, Food Science Building, 100 Cedar St., Athens, Georgia 30602., Duff MR Jr; Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee., Howell EE; Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee., Reyes-De-Corcuera JI; Department of Food Science and Technology, University of Georgia, Food Science Building, 100 Cedar St., Athens, Georgia 30602.
المصدر:	Biotechnology and bioengineering [Biotechnol Bioeng] 2017 Mar; Vol. 114 (3), pp. 516-525. Date of Electronic Publication: 2016 Sep 27.
نوع المنشور:	Journal Article
اللغة:	English
بيانات الدورية:	Publisher: Wiley Country of Publication: United States NLM ID: 7502021 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-0290 (Electronic) Linking ISSN: 00063592 NLM ISO Abbreviation: Biotechnol Bioeng Subsets: MEDLINE
أسماء مطبوعة:	Publication: <2005->: Hoboken, NJ : Wiley Original Publication: New York, Wiley.
مواضيع طبية MeSH:	Glucose Oxidase/chemistry , Glucose Oxidase/metabolism, Aniline Compounds ; Aspergillus niger/enzymology ; Benzoates ; Enzyme Stability ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Hydrophobic and Hydrophilic Interactions ; Hydrostatic Pressure ; Kinetics
مستخلص:	High hydrostatic pressure (HHP) stabilized glucose oxidase (GOx) against thermal inactivation. The apparent first-order kinetics of inactivation of GOx were investigated at 0.1-300 MPa and 58.8-80.0°C. At 240 MPa and 74.5°C, GOx inactivated at a rate 50 times slower than at atmospheric pressure at the same temperature. The apparent activation energy of inactivation at 300 MPa was 281.0 ± 17.4 kJ mol ^-1 or 1.3-fold smaller than for the inactivation at atmospheric pressure (378.1 ± 25.6 kJ mol ^-1 ). The stabilizing effect of HHP was greatest at 74.5°C, where the activation volume of 57.0 ± 12.0 cm ³ mol ^-1 was highest compared to all other studied temperatures. Positive apparent activation volumes for all the treatment temperatures confirmed that HHP favors GOx stabilization. A second approach to increase GOx stability involved crosslinking with N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC) and either aniline or benzoate. The modified enzyme remained fully active with only slight increases in K M (1.3-1.9-fold increases for aniline and benzoate modification, respectively). The thermal stability of GOx increased by 8°C with aniline modification, while it decreased by 0.9°C upon modification with benzoate. Biotechnol. Bioeng. 2017;114: 516-525. © 2016 Wiley Periodicals, Inc. (© 2016 Wiley Periodicals, Inc.)
فهرسة مساهمة:	Keywords: enzyme stabilization; glucose oxidase; high hydrostatic pressure; hydrophobic modification; inactivation kinetics
المشرفين على المادة:	0 (Aniline Compounds) 0 (Benzoates) 0 (Fungal Proteins) EC 1.1.3.4 (Glucose Oxidase) SIR7XX2F1K (aniline)
تواريخ الأحداث:	Date Created: 20160920 Date Completed: 20171017 Latest Revision: 20201209
رمز التحديث:	20240628
DOI:	10.1002/bit.26185
PMID:	27641970
قاعدة البيانات:	MEDLINE

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تدمد:	1097-0290
DOI:	10.1002/bit.26185