Employing Calorimetric Methods to Determine the Mechanism of the Invertase Maximal Activity Delay-Reference-Cited by-同舟云学术

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Employing Calorimetric Methods to Determine the Mechanism of the Invertase Maximal Activity Delay

Published:2020-12-16 Issue:1 Volume:1 Page:60-65
ISSN:2692-1944
Container-title:ACS Food Science & Technology
language:en
Short-container-title:ACS Food Sci. Technol.

Author:

Chan W. K. Dindi¹,Hicks Benjamin¹,Kaliappan Alagammai²,Garbett Nichola C.²,Hansen Lee D.³,Kenealey Jason D.¹^ORCID

Affiliation:

1. Department of Nutrition, Dietetic and Food Science, Brigham Young University, Provo, Utah 84602, United States

2. Department of Medicine, Division of Medical Oncology and Hematology, University of Louisville, Louisville, Kentucky 40202, United States

3. Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States

Funder

Brigham Young University

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acsfoodscitech.0c00011

Reference26 articles.

1. The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper

2. The Determination of Enzyme Dissociation Constants

3. A Note on the Kinetics of Enzyme Action

4. Calorimetric investigations of the enzyme catalyzed sucrose hydrolysis

5. Sucrose hydrolysis by invertase. Characterization of products and substrate inhibition

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Development of ZnO nanoflowers-assisted DNAzyme-based electrochemical platform for invertase and glucose oxidase-dominated biosensing;Analytica Chimica Acta;2022-11

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