• Molecules and Cells
• /
• v.38 no.5
• /
• pp.409-415
• /
• 2015

Low-barrier hydrogen bonds (LBHBs) have been proposed to have important influences on the enormous reaction rate increases achieved by many enzymes. ${\Delta}^5$-3-ketosteroi isomerase (KSI) catalyzes the allylic isomerization of ${\Delta}^5$-3-ketosteroid to its conjugated ${\Delta}^4$-isomers at a rate that approache the diffusion limit. Tyr14, a catalytic residue of KSI, has been hypothesized to form an LBHB with the oxyanion of a dienolate steroid intermediate generated during the catalysis. The unusual chemical shift of a proton at 16.8 ppm in the nuclear magnetic resonance spectrum has been attributed to an LBHB between Tyr14 $O{\eta}$ and C3-O of equilenin an intermediate analogue, in the active site of D38N KSI. This shift in the spectrum was not observed in Y30F/Y55F/D38N and Y30F/Y55F/Y115F/D38N mutant KSIs when each mutant was complexed with equilenin, suggesting that Tyr14 could not form LBHB with the intermediate analogue in these mutant KSIs. The crystal structure of Y30F/Y55F/Y115F/D38N-equilenin complex revealed that the distance between Tyr14 $O{\eta}$ and C3-O of the bound steroi was within a direct hydrogen bond. The conversion of LBHB to an ordinary hydrogen bond in the mutant KSI reduced the binding affinity for the steroid inhibitors by a factor of 8.1-11. In addition, the absence of LBHB reduced the catalytic activity by only a factor of 1.7-2. These results suggest that the amount of stabilization energy of the reaction intermediate provided by LBHB is small compared with that provided by an ordinary hydrogen bond in KSI.

• Journal of the Korean Chemical Society
• /
• v.21 no.2
• /
• pp.83-88
• /
• 1977

Kinetic studies on the rates of reactions of 2, 4-dinitrochlorobenzene with p-toluidine, aniline and p-chloroaniline in $CH_3CH-CH_3OH$ binary solvent mixtures have been carried out. The experimental results have been explained in terms of the specific solvation by alcoholic hydrogen. It has been shown that the bond breaking step is rate determining in the solvent system studied and the energy barrier is getting low as the solvent changes from acetonitrile to methanol.

• 한국유가공학회:학술대회논문집
• /
• 2002.04a
• /
• pp.59-60
• /
• 2002

Edible films such as wax coatings, sugar and chocolate covers, and sausage casings, have been used in food applications for years$^{(1)}$ However, interest in edible films and biodegradable polymers has been renewed due to concerns about the environment, a need to reduce the quantity of disposable packaging, and demand by the consumer for higher quality food products. Edible films can function as secondary packaging materials to enhance food quality and reduce the amount of traditional packaging needed. For example, edible films can serve to enhance food quality by acting as moisture and gas barriers, thus, providing protection to a food product after the primary packaging is opened. Edible films are not meant to replace synthetic packaging materials; instead, they provide the potential as food packagings where traditional synthetic or biodegradable plastics cannot function. For instance, edible films can be used as convenient soluble pouches containing single-servings for products such as instant noodles and soup/seasoning combination. In the food industry, they can be used as ingredient delivery systems for delivering pre-measured ingredients during processing. Edible films also can provide the food processors with a variety of new opportunities for product development and processing. Depends on materials of edible films, they also can be sources of nutritional supplements. Especially, whey proteins have excellent amino acid balance while some edible films resources lack adequate amount of certain amino acids, for example, soy protein is low in methionine and wheat flour is low in lysine$^{(2)}$. Whey proteins have a surplus of the essential amino acid lysine, threonine, methionine and isoleucine. Thus, the idea of using whey protein-based films to individually pack cereal products, which often deficient in these amino acids, become very attractive$^{(3)}$. Whey is a by-product of cheese manufacturing and much of annual production is not utilized$^{(4)}$. Development of edible films from whey protein is one of the ways to recover whey from dairy industry waste. Whey proteins as raw materials of film production can be obtained at inexpensive cost. I hypothesize that it is possible to make whey protein-based edible films with improved moisture barrier properties without significantly altering other properties by producing whey protein/lipid emulsion films and these films will be suitable far food applications. The fellowing are the specific otjectives of this research: 1. Develop whey protein/lipid emulsion edible films and determine their microstructures, barrier (moisture and oxygen) and mechanical (tensile strength and elongation) properties. 2. Study the nature of interactions involved in the formation and stability of the films. 3. Investigate thermal properties, heat sealability, and sealing properties of the films. 4. Demonstrate suitability of their application in foods as packaging materials. Methodologies were developed to produce edible films from whey protein isolate (WPI) and concentrate (WPC), and film-forming procedure was optimized. Lipids, butter fat (BF) and candelilla wax (CW), were added into film-forming solutions to produce whey protein/lipid emulsion edible films. Significant reduction in water vapor and oxygen permeabilities of the films could be achieved upon addition of BF and CW. Mechanical properties were also influenced by the lipid type. Microstructures of the films accounted for the differences in their barrier and mechanical properties. Studies with bond-dissociating agents indicated that disulfide and hydrogen bonds, cooperatively, were the primary forces involved in the formation and stability of whey protein/lipid emulsion films. Contribution of hydrophobic interactions was secondary. Thermal properties of the films were studied using differential scanning calorimetry, and the results were used to optimize heat-sealing conditions for the films. Electron spectroscopy for chemical analysis (ESCA) was used to study the nature of the interfacial interaction of sealed films. All films were heat sealable and showed good seal strengths while the plasticizer type influenced optimum heat-sealing temperatures of the films, 130$^{\circ}$C for sorbitol-plasticized WPI films and 110$^{\circ}$C for glycerol-plasticized WPI films. ESCA spectra showed that the main interactions responsible for the heat-sealed joint of whey protein-based edible films were hydrogen bonds and covalent bonds involving C-0-H and N-C components. Finally, solubility in water, moisture contents, moisture sorption isotherms and sensory attributes (using a trained sensory panel) of the films were determined. Solubility was influenced primarily by the plasticizer in the films, and the higher the plasticizer content, the greater was the solubility of the films in water. Moisture contents of the films showed a strong relationship with moisture sorption isotherm properties of the films. Lower moisture content of the films resulted in lower equilibrium moisture contents at all aw levels. Sensory evaluation of the films revealed that no distinctive odor existed in WPI films. All films tested showed slight sweetness and adhesiveness. Films with lipids were scored as being opaque while films without lipids were scored to be clear. Whey protein/lipid emulsion edible films may be suitable for packaging of powder mix and should be suitable for packaging of non-hygroscopic foods$^{(5,6,7,8,)}$.

• Proceedings of the Korean Vacuum Society Conference
• /
• 2013.08a
• /
• pp.91-91
• /
• 2013

Imagine a world where we could biomanufacture hybrid nanomaterials having atomic-scale resolution over functionality and architecture. Toward this vision, a fundamental challenge in materials science is how to design and synthesize protein-like material that can be fully self-assembled and exhibit information-specific process. In an ongoing effort to extend the fundamental understanding of protein structure to non-natural systems, we have designed a class of short peptides to fold like proteins and assemble into defined nanostructures. In this talk, I will talk about new strategies to drive the self-assembled structures designing sequence of peptide. I will also discuss about the specific interaction between proteins and inorganics that can be used for the development of new hybrid solar energy devices. Splitting water into hydrogen and oxygen is one of the promising pathways for solar to energy convertsion and storage system. The oxygen evolution reaction (OER) has been regarded as a major bottleneck in the overall water splitting process due to the slow transfer rate of four electrons and the high activation energy barrier for O-O bond formation. In nature, there is a water oxidation complex (WOC) in photosystem II (PSII) comprised of the earthabundant elements Mn and Ca. The WOC in photosystem II, in the form of a cubical CaMn4O5 cluster, efficiently catalyzes water oxidation under neutral conditions with extremely low overpotential (~160 mV) and a high TOF number. The cluster is stabilized by a surrounding redox-active peptide ligand, and undergo successive changes in oxidation state by PCET (proton-coupled electron transfer) reaction with the peptide ligand. It is fundamental challenge to achieve a level of structural complexity and functionality that rivals that seen in the cubane Mn4CaO5 cluster and surrounding peptide in nature. In this presentation, I will present a new strategy to mimic the natural photosystem. The approach is based on the atomically defined assembly based on the short redox-active peptide sequences. Additionally, I will show a newly identified manganese based compound that is very close to manganese clusters in photosystem II.