denaturation

(redirected from Protein denaturation)
Also found in: Encyclopedia.

denaturation

 [de-na″chur-a´shun]
a change in the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking, or the change in the physical properties of a substance, such as a protein or nucleic acid, caused by heat or certain chemicals that alter tertiary structure.
protein denaturation any nonproteolytic change in the chemistry, composition, or structure of a native protein that causes it to lose some or all of its unique or specific characteristics.

de·na·tur·a·tion

(dē-na'tyū-rā'shŭn),
The process of becoming denatured.

denaturation

/de·na·tur·a·tion/ (de-na″cher-a´shun) destruction of the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking, or the change in the physical properties of a substance, as a protein or nucleic acid, caused by heat or certain chemicals that alter tertiary structure.

denaturation

[dēnā′chərā′shən]
Etymology: L, de + natura, natural
1 the alteration of the basic nature or structure of a substance.
2 the process of making a potential food or beverage substance unfit for human consumption although it may still be used for other purposes, such as a solvent.

de·na·tur·a·tion

(dē-nā'chŭr-ā'shŭn)
The process of becoming denatured.

denaturation

1. Alteration in the folding pattern of a protein by heat or chemical reaction from its physiological conformation to an inactive shape.
2. In the case of DNA or RNA the conversion from a double-stranded structure to a single stranded structure, usually by heating. This is an essential stage in the POLYMERASE CHAIN REACTION.

denaturation

the breakdown of the bonds forming the quaternary, tertiary and secondary structures of PROTEINS and NUCLEIC ACIDS, a process that can be caused by various agents, such as excess heat, strong acids or alkalis, organic solvents and ultrasonic vibration. In some cases, denaturation is irreversible as in, for example, the heating of egg albumen to give solid egg white. When denaturation occurs in enzymes, they are inactivated, with major effects in living organisms. Denatured nucleic acids can often be returned to their original configuration in the process of renaturation.

denaturation

1. a change in the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking.
2. in proteins and nucleic acids produced by heat or certain chemicals, usually results in loss of function. In proteins, various noncovalent bonds are disrupted resulting in unfolding of the polypeptide chain; in nucleic acids hydrogen bonds between nucleotides are disrupted converting double-stranded molecules or parts of them into single-stranded forms.

protein denaturation
any nonproteolytic change in the chemistry, composition or structure of a native protein which causes it to lose some or all of its unique or specific characteristics.
References in periodicals archive ?
By preventing the use of excessive temperatures, the risk of protein denaturation will be reduced.
At 56 [degrees]C, the activity dropped rapidly, probably as a result of protein denaturation.
This occurs because of the higher activation energy of meat protein denaturation, compared with the lower activation energy of disrupting the most vulnerable bacterial enzymes.
More than 20 papers are reproduced here and their titles run: Potential and physical properties of underutilized species, Menhaden; Trimethylamine-N-oxide demethylation and protein denaturation in fish muscle; Factors affecting physical properties of fish protein gel; The implications of omega-3 fatty acids in human health; Lipid oxidation in fish muscle; Recovery of pigments and chitin from pink shrimp peeling wastes; Enzyme preservation of fresh seafoods; Supercritical fluid C|O.
Ultra-high pressure causes whey protein denaturation as well as partial disruption of the casein micelles.
As boiling time increased, dense protein structure occurred due to protein denaturation and aggregation; the gap regions were also more frequently observed around the muscle fibres.
In yogurt manufacture, milk undergoes a very high heat treatment to cause whey protein denaturation and its association with casein micelles.
effects on different functional food characteristics such as starch gelatinization, protein denaturation, and enzyme inactivation.
That step took more than 50 hours to complete, resulting in protein denaturation and thus product recovery of only 50 percent.
Protein denaturation as a result of [gamma]-irradiation increased in vitro CP digestibility of irradiated SB at doses of 30 and 45 kGy by 12 and 28%, respectively.