Characterization of Afp1, an Antifreeze Protein from the Psychrophilic Yeast Glaciozyma Antarctica PI12

Overview

Journal Extremophiles

Publisher Springer

Date 2012 Nov 8

PMID 23132550

Citations 27

Authors

Noor Haza Fazlin Hashim

Izwan Bharudin

Douglas Law Sie Nguong

Sakura Higa

Farah Diba Abu Bakar

Sheila Nathan

Amir Rabu

Hidehisa Kawahara

Rosli Md Illias

Nazalan Najimudin

Nor Muhammad Mahadi

Abdul Munir Abdul Murad

Affiliations

Soon will be listed here.

Abstract

The psychrophilic yeast Glaciozyma antarctica demonstrated high antifreeze activity in its culture filtrate. The culture filtrate exhibited both thermal hysteresis (TH) and ice recrystallization inhibition (RI) properties. The TH of 0.1 °C was comparable to that previously reported for bacteria and fungi. A genome sequence survey of the G. antarctica genome identified a novel antifreeze protein gene. The cDNA encoded a 177 amino acid protein with 30 % similarity to a fungal antifreeze protein from Typhula ishikariensis. The expression levels of AFP1 were quantified via real time-quantitative polymerase chain reaction (RT-qPCR), and the highest expression levels were detected within 6 h of growth at -12 °C. The cDNA of the antifreeze protein was cloned into an Escherichia coli expression system. Expression of recombinant Afp1 in E. coli resulted in the formation of inclusion bodies that were subsequently denatured by treatment with urea and allowed to refold in vitro. Activity assays of the recombinant Afp1 confirmed the antifreeze protein properties with a high TH value of 0.08 °C.

Citing Articles

Antifreeze proteins produced by Antarctic yeast from the genus Glaciozyma as cryoprotectants in food storage.

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Freezing and thawing in Antarctica: characterization of antifreeze protein (AFP) producing microorganisms isolated from King George Island, Antarctica.

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