US 6,747,130 B2 · Tenebrio antifreeze proteins

Abstract

A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 μg/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ˜1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

Claims17

Dependent claims

An isolated or recombinantly expressed antifreeze protein, said protein comprising the following:

(i) a calculated molecular weight of between 7 and 13 kDa;
(ii) a thermal hysteresis activity of greater than 1.5° C. at a concentration of about 1 mg/mL;
(iii) the N-terminal amino acid motif set forth in SEQ ID NO:
3;
(iv) at least 70% amino acid sequence identity to the antifreeze protein YL-I (SEQ ID NO:
11);
and
(v) 4 repeats of the 12 contiguous amino acid motif set forth in SEQ ID NO:
1.

6 more elements

Dependencies are inferred from the claim text.

Tenebrio antifreeze proteins

Life of this patent

Tenebrio antifreeze proteins

Life of this patent

Abstract

Claims17