Abstract
A new recombinant Picrophilus torridus TSase (PTTS) has the catalytic ability for the conversion of maltose to trehalose by intramolecular transglucosylation. For industrial applications, the high thermostability of the enzyme would be the most important property for reducing the microbial contamination and lower the production cost. Therefore, in this study, we substituted ten selected proline residues of PTTS which differ from two well-known thermostable TSases. Interestingly, we found that the N503 mutant type, namely N503P-PTTS, showed about 39% higher relative activity than that of the wild type at 65 °C for 120 min. The trehalose yield of mutant N503P-PTTS was 1.3-fold higher than that of the wild type with sweet potato starch as substrate at 50 °C for 4 h. This suggests that the proline site substitution technology used in this study is useful for altering enzyme properties and catalytic efficiency for possible industrial applications.
| Original language | English |
|---|---|
| Pages (from-to) | 1017-1022 |
| Number of pages | 6 |
| Journal | Food Chemistry |
| Volume | 119 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2010 Apr 1 |
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Keywords
- Amylase
- Maltose
- Mutation
- Proline
- Sweet potato
- Thermostability
- Trehalose
- Trehalose synthase
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science
Cite this
Site-directed mutagenesis improves the thermostability of a recombinant Picrophilus torridus trehalose synthase and efficiency for the production of trehalose from sweet potato starch. / Chou, Hsin Hung; Chang, Shu Wei; Lee, Guan-Chiun; Chen, Yi Shan; Yeh, Tzunuan; Akoh, Casimir C.; Shaw, Jei Fu.
In: Food Chemistry, Vol. 119, No. 3, 01.04.2010, p. 1017-1022.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Site-directed mutagenesis improves the thermostability of a recombinant Picrophilus torridus trehalose synthase and efficiency for the production of trehalose from sweet potato starch
AU - Chou, Hsin Hung
AU - Chang, Shu Wei
AU - Lee, Guan-Chiun
AU - Chen, Yi Shan
AU - Yeh, Tzunuan
AU - Akoh, Casimir C.
AU - Shaw, Jei Fu
PY - 2010/4/1
Y1 - 2010/4/1
N2 - A new recombinant Picrophilus torridus TSase (PTTS) has the catalytic ability for the conversion of maltose to trehalose by intramolecular transglucosylation. For industrial applications, the high thermostability of the enzyme would be the most important property for reducing the microbial contamination and lower the production cost. Therefore, in this study, we substituted ten selected proline residues of PTTS which differ from two well-known thermostable TSases. Interestingly, we found that the N503 mutant type, namely N503P-PTTS, showed about 39% higher relative activity than that of the wild type at 65 °C for 120 min. The trehalose yield of mutant N503P-PTTS was 1.3-fold higher than that of the wild type with sweet potato starch as substrate at 50 °C for 4 h. This suggests that the proline site substitution technology used in this study is useful for altering enzyme properties and catalytic efficiency for possible industrial applications.
AB - A new recombinant Picrophilus torridus TSase (PTTS) has the catalytic ability for the conversion of maltose to trehalose by intramolecular transglucosylation. For industrial applications, the high thermostability of the enzyme would be the most important property for reducing the microbial contamination and lower the production cost. Therefore, in this study, we substituted ten selected proline residues of PTTS which differ from two well-known thermostable TSases. Interestingly, we found that the N503 mutant type, namely N503P-PTTS, showed about 39% higher relative activity than that of the wild type at 65 °C for 120 min. The trehalose yield of mutant N503P-PTTS was 1.3-fold higher than that of the wild type with sweet potato starch as substrate at 50 °C for 4 h. This suggests that the proline site substitution technology used in this study is useful for altering enzyme properties and catalytic efficiency for possible industrial applications.
KW - Amylase
KW - Maltose
KW - Mutation
KW - Proline
KW - Sweet potato
KW - Thermostability
KW - Trehalose
KW - Trehalose synthase
UR - http://www.scopus.com/inward/record.url?scp=70449536409&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70449536409&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2009.08.010
DO - 10.1016/j.foodchem.2009.08.010
M3 - Article
AN - SCOPUS:70449536409
VL - 119
SP - 1017
EP - 1022
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
IS - 3
ER -