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Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21

หน่วยงาน มหาวิทยาลัยเชียงใหม่

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ชื่อเรื่อง : Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21
นักวิจัย : Kanpiengjai A. , Nguyen T. , Haltrich D. , Khanongnuch C.
คำค้น : -
หน่วยงาน : มหาวิทยาลัยเชียงใหม่
ผู้ร่วมงาน : -
ปีพิมพ์ : 2560
อ้างอิง : 01418130 , 2-s2.0-85020289348 , 10.1016/j.ijbiomac.2017.05.168 , https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85020289348&origin=inward , http://cmuir.cmu.ac.th/jspui/handle/6653943832/40094
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : -
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

© 2017 Elsevier B.V. Lactobacillus plantarum S21 α-amylase possesses 475 amino acids at the C-terminal region identified as the starch-binding domain (SBD) and has been previously reported to play a role in raw starch degradation. To understand the specific roles of this SBD, cloning and expression of the complete (AmyL9) and C-terminally truncated (AmyL9Δ SBD ) forms of α-amylase were conducted for enzyme purification and comparative characterization. AmyL9 and AmyL9Δ SBD were overproduced in Escherichia coli at approximately 10- and 20-times increased values of volumetric productivity when compared to α-amylase produced by the wild type, respectively. AmyL9Δ SBD was unable to hydrolyze raw starch and exhibited substrate specificity in a similar manner to that of AmyL9, but it was weakly active toward amylopectin and glycogen. The hydrolysis products obtained from the amylaceous substrates of both enzymes were the same. In addition, AmyL9Δ SBD showed comparatively higher K m values than AmyL9 when it reacted with starch and amylopectin, and lower values for other kinetic constants namely v max , k cat , and k cat /K m . The results indicated that the C-terminal SBDs of L. plantarum S21 α-amylase contribute to not only substrate preference but also substrate affinity and the catalytic efficiency of the α-amylase without any changes in the degradation mechanisms of the enzyme.

บรรณานุกรม :
Kanpiengjai A. , Nguyen T. , Haltrich D. , Khanongnuch C. . (2560). Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21.
    เชียงใหม่ : มหาวิทยาลัยเชียงใหม่ .
Kanpiengjai A. , Nguyen T. , Haltrich D. , Khanongnuch C. . 2560. "Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21".
    เชียงใหม่ : มหาวิทยาลัยเชียงใหม่ .
Kanpiengjai A. , Nguyen T. , Haltrich D. , Khanongnuch C. . "Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21."
    เชียงใหม่ : มหาวิทยาลัยเชียงใหม่ , 2560. Print.
Kanpiengjai A. , Nguyen T. , Haltrich D. , Khanongnuch C. . Expression and comparative characterization of complete and C-terminally truncated forms of saccharifying α-amylase from Lactobacillus plantarum S21. เชียงใหม่ : มหาวิทยาลัยเชียงใหม่ ; 2560.