Protein engineering to change thermal stability for food enzymes

1991 ◽  
Vol 19 (3) ◽  
pp. 655-662 ◽  
Author(s):  
Peter W. Goodenough ◽  
John A. Jenkins

Summary In this review we have briefly indicated how the present state of knowledge allows proteins to be mutated to increase or decrease stability. We have discussed experiments on both model proteins and those of relevance to the food industry, and show how hydrophobic forces are a major driving force for folding as well as having a major role in thermostability. We have also indicated the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulphide bridges make to thermostability.

2001 ◽  
Vol 13 (5) ◽  
pp. 619-625 ◽  
Author(s):  
Alex Fragoso ◽  
Roberto Cao ◽  
Alicia Díz ◽  
Ileana Sånchez ◽  
Leticia Sånchez

CrystEngComm ◽  
2015 ◽  
Vol 17 (20) ◽  
pp. 3768-3771 ◽  
Author(s):  
Antonio Bauzá ◽  
Antonio Frontera ◽  
Tiddo J. Mooibroek ◽  
Jan Reedijk

A CSD analysis and DFT study reveal that the nitrogen lone-pair in [N(PPh3)2]+ is partially intact and involved in intramolecular hydrogen bonding.


Author(s):  
Bruce C. Bunker ◽  
William H. Casey

Water is one of the most complex fluids on Earth. Even after intense study, there are many aspects regarding the structure, properties, and chemistry of water that are not well understood. In this chapter, we highlight the attributes of water that dictate many of the reactions that take place between water and oxides. We start with a single water molecule and progress to water clusters, then finally to extended liquid and solid phases. This chapter provides a baseline for evaluating what happens when water encounters simple ions, soluble oxide complexes called hydrolysis products, and extended oxide phases. The primary phenomenon highlighted in this chapter is hydrogen bonding. Hydrogen bonding dominates the structure and properties of water and influences many water–oxide interactions. A single water molecule has eight valence electrons around a central oxygen anion. These electrons are contained in four sp3-hybridized molecular orbitals arranged as lobes that extend from the oxygen in a tetrahedral geometry. Each orbital is occupied by two electrons. Two of the lobes are bonded to protons; the other two lobes are referred to as lone pairs of electrons. The H–O–H bond angle of 104.5° is close to the tetrahedral angle of 109.5°. The O–H bond length in a single water molecule is 0.96 Ǻ. It is important to recognize that this bond length is really a measure of the electron density associated with the oxygen lone pair bonded to the proton. This is because a proton is so incredibly small (with an ionic radius of only 1.3·10−5 Ǻ) that it makes no contribution to the net bond length. The entire water molecule has a hard sphere diameter of 2.9 Ǻ, which is fairly typical for an oxygen anion. This means the unoccupied lone pairs are distended relative to the protonated lone pairs, extending out to roughly 1.9 Ǻ. The unequal distribution of charges introduces a dipole within the water molecule that facilitates electrostatic interactions with other molecules.


2021 ◽  
Vol 1225 ◽  
pp. 129090
Author(s):  
Himabindu Battula ◽  
Anwarhussaini SD ◽  
Smriti Arvind Nahata ◽  
Lipi Deepaakshi Patnaik ◽  
Santosh Ranga ◽  
...  

Antioxidants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 422
Author(s):  
Patrizia Casella ◽  
Angela Iovine ◽  
Sanjeet Mehariya ◽  
Tiziana Marino ◽  
Dino Musmarra ◽  
...  

Haematococcus pluvialis microalgae is a promising source of astaxanthin, an excellent antioxidant carotenoid. H. pluvialis, as well as other species, could find more extensive applications as healthy food for a variegated carotenoids composition in addition to astaxanthin. Official method has not currently been used for this purpose. The objective of this work was to propose a method to characterize carotenoids in H. pluvialis after the comparison between spectrophotometric and liquid chromatography analysis. In addition, in order to improve the use of astaxanthin in the food industry, thermal stability was investigated. In this context, the effect of temperature at 40–80 °C, over a 16 h storage period was tested on astaxanthin produced by H. pluvialis. A further test was carried out at room temperature (20 °C) for seven days. A decrease in the astaxanthin concentration was observed at all tested temperatures with a decrease >50% of all-trans isomer at 80 °C after 16 h and an increase of 9-cis and 13-cis isomers. In conclusion, the obtained results showed the importance of evaluating the degradation effect of temperature on astaxanthin used as a food additive for a future greater enhancement of this bioproduct in the food field.


2009 ◽  
Vol 9 (12) ◽  
pp. 5009-5013 ◽  
Author(s):  
Marcos D. García ◽  
Víctor Blanco ◽  
Carlos Platas-Iglesias ◽  
Carlos Peinador ◽  
José M. Quintela

2017 ◽  
Vol 50 (22) ◽  
pp. 9058-9065 ◽  
Author(s):  
Hongbo Yuan ◽  
Jialiang Xu ◽  
Eliane P. van Dam ◽  
Giulia Giubertoni ◽  
Yves L. A. Rezus ◽  
...  

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