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1.
Ultrason Sonochem ; 73: 105501, 2021 May.
Article in English | MEDLINE | ID: mdl-33676157

ABSTRACT

Ultrasonic emulsification (USE) assisted by cavitation is an effective method to produce emulsion droplets. However, the role of gas bubbles in the USE process still remains unclear. Hence, in the present paper, high-speed camera observations of bubble evolution and emulsion droplets formation in oil and water were used to capture in real-time the emulsification process, while experiments with different gas concentrations were carried out to investigate the effect of gas bubbles on droplet size. The results show that at the interface of oil and water, gas bubbles with a radius larger than the resonance radius collapse and sink into the water phase, inducing (oil-water) blended liquid jets across bubbles to generate oil-in-water-in-oil (O/W/O) and water-in-oil (W/O) droplets in the oil phase and oil-in-water (O/W) droplets in the water phase, respectively. Gas bubbles with a radius smaller than the resonance radius at the interface always move towards the oil phase, accompanied with the generation of water droplets in the oil phase. In the oil phase, gas bubbles, which can attract bubbles nearby the interface, migrate to the interface of oil and water due to acoustic streaming, and generate numerous droplets. As for the gas bubbles in the water phase, those can break neighboring droplets into numerous finer ones during bubble oscillation. With the increase in gas content, more bubbles undergo chaotic oscillation, leading to smaller and more stable emulsion droplets, which explains the beneficial role of gas bubbles in USE. Violently oscillating microbubbles are, therefore, found to be the governing cavitation regime for emulsification process. These results provide new insights to the mechanisms of gas bubbles in oil-water emulsions, which may be useful towards the optimization of USE process in industry.

2.
Ultrason Sonochem ; 52: 455-467, 2019 Apr.
Article in English | MEDLINE | ID: mdl-30594518

ABSTRACT

Ultrasonic (cavitation) melt processing attracts considerable interest from both academic and industrial communities as a promising route to provide clean, environment friendly and energy efficient solutions for some of the core issues of the metal casting industry, such as improving melt quality and providing structure refinement. In the last 5 years, the authors undertook an extensive research programme into fundamental mechanisms of cavitation melt processing using state-of-the-art and unique facilities and methodologies. This overview summarises the recent results on the evaluation of acoustic pressure and melt flows in the treated melt, direct observations and quantitative analysis of cavitation in liquid aluminium alloys, in-situ and ex-situ studies of the nucleation, growth and fragmentation of intermetallics, and de-agglomeration of particles. These results provide valuable new insights and knowledge that are essential for upscaling ultrasonic melt processing to industrial level.

3.
J Mol Evol ; 49(6): 819-21, 1999 Dec.
Article in English | MEDLINE | ID: mdl-10594185

ABSTRACT

The most comprehensive studies on a plant lysozyme (EC 3.2.1.17) are those on the enzyme from papaya (Carica papaya) latex, published in 1967 and 1969. However, the N-terminal amino acid sequence of five amino acid sequence of this enzyme, determined by manual Edman degradation, did not allow assignment to any of the much later-classified families of glycosyl hydrolases. N-Terminal sequence analysis of 22 residues of papaya lysozyme now shows unambiguously that the enzyme belongs to the family 19 chitinases. It has properties similar to those of basic class I chitinases with lysozyme activity, such as cleavage specificity at the C-1 of N-acetylmuramic acid with inversion of configuration, but as it lacks an N-terminal hevein domain, it should be classified as a class II chitinase.


Subject(s)
Chitinases/chemistry , Chitinases/classification , Evolution, Molecular , Muramidase/chemistry , Muramidase/classification , Rosales/enzymology , Amino Acid Sequence , Chitinases/isolation & purification , Databases, Factual , Magnoliopsida/enzymology , Molecular Sequence Data , Muramidase/isolation & purification , Sequence Analysis, Protein , Sequence Homology, Amino Acid
4.
Phytochemistry ; 43(1): 29-37, 1996 Sep.
Article in English | MEDLINE | ID: mdl-8987504

ABSTRACT

The lutoid-body (bottom) fraction of latex from the rubber tree (Hevea brasiliensis) contains a limited number of major proteins. These are, besides the chitin-binding protein hevein, its precursor and the C-terminal fragment of this precursor, proteins with enzymic activities: three hevamine components, which are basic, vacuolar, chitinases with lysozyme activity, and a beta-1,3-glucanase. Lutoid-body fractions from three rubber-tree clones differed in their contents of these enzyme proteins. The hevamine components and glucanase were isolated and several enzymic and structural properties were investigated. These enzymes are basic proteins and cause coagulation of the negatively charged rubber particles. The coagulation occurs in a rather narrow range of ratios of added protein to rubber particles, which indicates that charg neutralization is the determining factor. Differences in coagulation of rubber particles by lutoid-body fractions from various rubber clones can be explained by their content of hevamine and glucanase. Glucanase from the lutoid-body fraction may dissolve callus tissue and this may explain the observation that rubber-tree clones with a high glucanase content in this fraction produce more latex than clones with little glucanase. Sequence studies of two CNBr peptides of the glucanase indicate that this protein is homologous with glucanases from other plants, and that a C-terminal peptide, possibly involved in vacuolar targeting, may have been cleaved off.


Subject(s)
Chitinases/isolation & purification , Trees/enzymology , beta-Glucosidase/isolation & purification , Amino Acid Sequence , Chitinases/metabolism , Chromatography, DEAE-Cellulose , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Glucan 1,3-beta-Glucosidase , Molecular Sequence Data , Sequence Homology, Amino Acid , beta-Glucosidase/metabolism
5.
FEBS Lett ; 363(3): 211-3, 1995 Apr 24.
Article in English | MEDLINE | ID: mdl-7737403

ABSTRACT

The 20 kDa precursor of hevein and its C-terminal 14 kDa domain have been isolated. Sequence analysis of the C-terminal tryptic peptides of these proteins and comparison with the cDNA sequence indicate that they represent mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, has been removed. The molar ratio of hevein to the C-terminal domain in the lutoid-body fraction of rubber latex is about 30:1. This indicates that not only the pre- and propeptides but also the 14 kDa domain are removed by proteolysis or other processes in the latex vessel after the processing of hevein has taken place.


Subject(s)
Antimicrobial Cationic Peptides , Lectins/metabolism , Plant Proteins/metabolism , Amino Acid Sequence , Latex/chemistry , Molecular Sequence Data , Plant Lectins , Protein Precursors/metabolism , Protein Processing, Post-Translational , Sequence Alignment , Sequence Homology, Amino Acid , Trees
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