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This book will be of interest of scholars and academics of Food Science, Chemistry, Biochemistry, Pharmacy, Medicine fields, among others. Tannic acid (TA) is a bioactive molecule that shows some functional properties, such as antidiabetic, antimutagenic, and antimicrobial activities. However, it also presents some limitations like bitter taste and astringent sensation on the palate, which reduces its acceptance by consumers. TA can form complexes with proteins and this ability may be useful to deliver this important molecule in different matrices. In this book, we relate the determination of thermodynamic parameters of TA-proteins complex formation. The thermodynamic properties of complexes formation in general and specifically the driving force of the TA-protein interaction were dependent on the chemical structure of the biopolymers. TA can perform the molecular recognition process of both hydrophilic and hydrophobic sites. The knowledge about the thermodynamic parameters can provide information to understand driving forces to form complexes with TA and, consequently, to select the better protein to carry TA or to develop nutraceuticals for better starch digestion. Edited by Ana Clarissa dos Santos Pires, Associated Professor of Food Technology Department of Federal University of Vicosa and Luis Henrique Mendes da Silva, Full Professor of Chemistry Department of Federal University of Vicosa, Brazil. Contributors include: Talma Duarte Freitas, Eliara Acipreste Hudson, Jaqueline de Paula Rezende, Yara Luiza Coelho, Marcia Cristina Teixeira Ribeiro Vidigal.
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This book will be of interest of scholars and academics of Food Science, Chemistry, Biochemistry, Pharmacy, Medicine fields, among others. Tannic acid (TA) is a bioactive molecule that shows some functional properties, such as antidiabetic, antimutagenic, and antimicrobial activities. However, it also presents some limitations like bitter taste and astringent sensation on the palate, which reduces its acceptance by consumers. TA can form complexes with proteins and this ability may be useful to deliver this important molecule in different matrices. In this book, we relate the determination of thermodynamic parameters of TA-proteins complex formation. The thermodynamic properties of complexes formation in general and specifically the driving force of the TA-protein interaction were dependent on the chemical structure of the biopolymers. TA can perform the molecular recognition process of both hydrophilic and hydrophobic sites. The knowledge about the thermodynamic parameters can provide information to understand driving forces to form complexes with TA and, consequently, to select the better protein to carry TA or to develop nutraceuticals for better starch digestion. Edited by Ana Clarissa dos Santos Pires, Associated Professor of Food Technology Department of Federal University of Vicosa and Luis Henrique Mendes da Silva, Full Professor of Chemistry Department of Federal University of Vicosa, Brazil. Contributors include: Talma Duarte Freitas, Eliara Acipreste Hudson, Jaqueline de Paula Rezende, Yara Luiza Coelho, Marcia Cristina Teixeira Ribeiro Vidigal.