Displaying of Trehalose Synthase Through Pichia pastoris and its Enzymatic Properties

doi:10.3969/j.issn.1673-1689.2016.01.009

Home > Archive>Volume 35, Issue 1, 2016 >59-65. DOI:10.3969/j.issn.1673-1689.2016.01.009

Displaying of Trehalose Synthase Through Pichia pastoris and its Enzymatic Properties
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                        10.3969/j.issn.1673-1689.2016.01.009
                    
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The study aimed to display trehalose synthase（TS.EC 5.4.99.16）on the surface of Pichiia pastoris and investigate its enzymatic properties. Synthesized gene from Streptomyces coelicolor trehalose synthase and yeast cell wall protein GCW14 was cloned to pPIC9k carrier and transformed into yeast GS115 and thus the pPIC9k-GCW14-TS carrier was constructed to display TS. Then the properties of the recombinant trehalose synthase were determined. Results showed that the recombinant trehalose synthase possessed the optimal temperature 30~45 ℃ and pH 8.5，K+ and Mg2+ increased its enzymatic capacity and more than 75% of the activity was still remained after it was reused for 5 times. Therefore，this recombinant strain can be repeatedly use as a whole cell catalyst to convert maltose into trehalose.

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SHENG Min, XIE Ding, WEN Li, JIAO Ling, JIANG Bo, FANG Fang. Displaying of Trehalose Synthase Through Pichia pastoris and its Enzymatic Properties[J]. Journal of Food Science and Biotechnology,2016,35(1):59-65.

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Online: March 11,2016
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