The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin

Liu, Wei; Zhang, Zhao-Qin; Xie, Mingyong; Tu, Zong–cai; Liu, Jianhua; Liang, Ruihong

doi:10.1016/j.foodchem.2010.04.079

Cited by 100 publications

(81 citation statements)

References 29 publications

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“…Because Trp residues of a protein are excited at 280 nm, the changes in the tertiary structure of the protein can be determined from the fluctuations of the fluorescence. [39,40] In plant protein, two aromatic amino acid residues, tryptophan (Trp) and tyrosine (Tyr), make the major contribution to the ultraviolet fluorescence of the protein. As the energy transfer from the tyrosine residues to the tryptophan residues leads to quenching of the fluorescence of the tyrosine residues and enhancement of the fluorescence of the tryptophan residues, it is generally accepted that the protein fluorescence results mainly from the fluorescence of Trp residues, whose peak position is between 325 and 350 nm.…”

Section: Fluorescence Spectrummentioning

confidence: 99%

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Zhou

Zhang

et al. 2017

International Journal of Food Properties

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The objective of this study was to determine the functional and structural properties of Maillard reaction products of mung bean [Vigna radiate (L.)] protein isolate with dextran obtained under the temperature of 80°C or 90°C with different times (0, 1, 2, 3, 4, 5, and 6 h). The mung bean protein isolate-dextran conjugate had better solubility, emulsifying activity, and emulsifying stability than mung bean protein isolate; however, the protein aggregation decreased the solubility, surface hydrophobicity, emulsifying activity, and emulsifying stability of mung bean protein isolate-dextran conjugate. In general, these functional properties of mung bean protein isolate-dextran conjugate obtained at 80°C with lower degree of glycosylation and browning degree were better than mung bean protein isolatedextran conjugate obtained at 90°C. Both vicilin (8S) and legumin type (11S) globulins both participated in the graft reaction, the subunit with a molecular weight of 21 kDa that contributed to 11S globulin might be the most vulnerable to dextran followed by the 60, 32, and 26 kDa subunits. Maillard reaction between mung bean protein isolate and dextran led to a decreased fluorescence intensity and a bathochromic shift. The fluorescence intensity of mung bean protein isolate-dextran conjugate generally decreased, and λ max of mung bean protein isolate-dextran conjugate first increased and then decreased. The grafted mung bean protein isolates had lower α-helix content but higher β-sheet content. As the Maillard reaction between mung bean protein isolate and dextran proceeded, the α-helix contents of the mung bean protein isolate-dextran conjugates were significantly increased and then decreased, and the β-sheet content generally decreased and then increased. Excessive grafted dextran and more protein aggregation was observed in mung bean protein isolate-dextran conjugate obtained at 90°C, which induced structural changes that might have impaired the functions. Our findings suggest that conjugation of mung bean protein isolate with dextran through the Maillard reaction is an effective way of improving the functional properties of mung bean protein isolate for its application in the food industry. ARTICLE HISTORY

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Section: Fluorescence Spectrummentioning

confidence: 99%

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Zhou

Zhang

et al. 2017

International Journal of Food Properties

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“…Generally, trypsin is isolated from the pancreas of mammals [14]. Trypsin has been commonly used in biological research during proteomics experiments.…”

Section: Introductionmentioning

confidence: 99%

Characterization and immobilization of trypsin on tannic acid modified Fe3O4 nanoparticles

Atacan

Özacar

2015

Colloids and Surfaces B: Biointerfaces

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“…DHPM is an emerging technology, which uses the combined forces of highvelocity impact, high-frequency vibration, instantaneous pressure drop, intense shear, cavitation, and ultra-high pressures up to 200 MPa with a short treatment time (<5 s) and continuous operation [27]. It has already been applied in microbial reduction, preparation of mozzarella cheese, improvement of whey protein, preparation of liposomes, preparation of nano-emulsions, and improvement of dietary fiber [28].…”

Section: Introductionmentioning

confidence: 99%

Effect of dynamic high‐pressure microfluidization on the morphology characteristics and physicochemical properties of maize amylose

Yue-bin

Wang

et al. 2012

Starch Stärke

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Maize amylose-water suspension (6% w/w) was subjected to single-pass dynamic highpressure microfluidization (DHPM) treatment at 80, 120, 160, and 200 MPa, and changes in the morphology characteristics and physicochemical properties were compared with native maize amylose as a control sample. Laser scattering measurements of particle size demonstrated with microfluidization treatment at 80 MPa showed a slight decrease in mean diameter, while a significant increase was observed above 120 MPa. SEM analysis showed that the surface appearances of maize amylose were altered and the starch granules were partially gelatinized after DHPM treatment. The microfluidization treated maize amylose showed elevated light transmittance and swelling power. However, the solubility was decreased and no significant changes in the freeze-thaw stability. DSC analysis showed a decrease in gelatinization temperatures (T o , T c ) and gelatinization enthalpy (DH) upon highpressure treatment. The texture profile analysis of the starch gel prepared from the suspension treated with high pressure obtained higher hardness and adhesiveness, lower cohesiveness and springiness. The results provide the basic information on the physicochemical properties of maize amylose treated at different microfluidized pressures and indicate the potential possibility of DHPM for starch modification.

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The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin

Cited by 100 publications

References 29 publications

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Characterization and immobilization of trypsin on tannic acid modified Fe3O4 nanoparticles

Effect of dynamic high‐pressure microfluidization on the morphology characteristics and physicochemical properties of maize amylose

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