2008
DOI: 10.2503/jjshs1.77.229
|View full text |Cite
|
Sign up to set email alerts
|

Purification and Biochemical Characterization of Cell Wall-bound Trehalase from Pericarp Tissues of Actinidia deliciosa

Abstract: A trehalase (EC 3.2.1.28) was purified from the cell walls of Actinidia deliciosa fruit. The purified trehalase had optimal pH of around 5, Km of 0.25 mM and Vmax of 5667 pkat/mg protein, and was relatively heat stable. The enzyme showed highly specific activity to trehalose and weak activity to maltose and maltotriose, but did not hydrolyze any other disaccharides. Trehalase activity was unaffected by Ca 2+ , Na, and Mg 2+ions and EDTA, but markedly inhibited by Hg 2+ and Fe 3+ ions, iodoacetic acid, tris(hyd… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
4
0

Year Published

2012
2012
2022
2022

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 5 publications
(4 citation statements)
references
References 16 publications
0
4
0
Order By: Relevance
“…An increased amount of trehalose, nonreducing disaccharide, in fruits has been reported to improve shelf life [41]. In this study, the gene that encodes trehalase (α-glucoside-1-glucohydrolase), a hydrolytic cell wall-bound enzyme that cleaves trehalose into two glucose moieties [41] was upregulated due to ethylene treatment. This phenomenon degrades apoplastic trehalose which in turn causes softening of the fruit ( Figure 5).…”
Section: Firmness and Genes Related To Softeningmentioning
confidence: 72%
See 1 more Smart Citation
“…An increased amount of trehalose, nonreducing disaccharide, in fruits has been reported to improve shelf life [41]. In this study, the gene that encodes trehalase (α-glucoside-1-glucohydrolase), a hydrolytic cell wall-bound enzyme that cleaves trehalose into two glucose moieties [41] was upregulated due to ethylene treatment. This phenomenon degrades apoplastic trehalose which in turn causes softening of the fruit ( Figure 5).…”
Section: Firmness and Genes Related To Softeningmentioning
confidence: 72%
“…In addition, the genes that encode aquaporin PIP1-4-like and aquaporin PIP2-7-like were downregulated probably due to the reduction of the transport of water and solutes across the cell membrane [46] as the fruit ripened. 7 wall-bound enzyme that cleaves trehalose into two glucose moieties [41] was upregulated due to ethylene treatment. This phenomenon degrades apoplastic trehalose which in turn causes softening of the fruit ( Figure 5).…”
Section: Firmness and Genes Related To Softeningmentioning
confidence: 99%
“…In plants, trehalase participates in the regulation of sucrose and starch, confers stress resistance [42], and participates in the formation and development of bean nodules. Trehalase has been found in chickpea (Cicer arietinum L.) seeds [43] and kiwi fruit (Actinidia deliciosa) [44].…”
Section: Animals and Plantsmentioning
confidence: 99%
“…Studies on the substrate specificity of most trehalases show that they are highly specific towards trehalose and have no catalytic effect on other disaccharides such as brown sugar, maltose, isomaltose, furanose, maltose, palatinose, and sucrose. The trehalase purified from the cell walls of Actinidia deliciosa fruit displayed weak activity with maltose and maltotriose [44]. Trehalase from Candida catalyzes on both trehalose and sucrose breakdown, and the ratio between trehalase and invertase activity is 1:3.5 [91].…”
Section: Substrate Specificitymentioning
confidence: 99%