当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Engineering a chimeric acid-stable α-amylase-glucoamylase (Amy-Glu) for one step starch saccharification.

Engineering a chimeric acid-stable α-amylase-glucoamylase (Amy-Glu) for one step starch saccharification.

Abstract：

:For saccharifying starch in one step, a chimeric biocatalyst (Amy-Glu) was generated from engineered α-amylase (Ba-Gt-amy) of Bacillus acidicola and glucoamylase (Glu) gene of Aspergillus niger. In order to join two enzymes, a linker peptide of 25 amino acids was used. Chimeric Amy-Glu was expressed in E. coli. Glu is of 75kDa, while Amy-Glu is of 145kDa. Both Amy-Glu and Glu displayed similar pH profile with good activity in the acidic pH range like that of Ba-Gt-amy with optimum at pH 4.0. All three enzymes (Ba-Gt-amy, Amy-Glu and glucoamylase) exhibited activity in the temperature range between 40 and 70°C with optimum at 60°C. Amy-Glu and Glu have T1/2 of 90 and 70min at 60 and 70°C, respectively. The Km, Vmax and Kcat values of Glu (soluble starch) are 0.34mgmL-1, 606μmolmg-1min-1 and 727s-1, while for Amy-Glu are 0.84mgmL-1, 13,886μmolmg-1min-1 and 4.2×104s-1, respectively. The end product analysis suggested that Amy-Glu retains the activity of both parental enzymes and forms maltodextrins along with glucose as the major products. Amy-Glu saccharifies wheat and corn starches more efficiently than the Ba-Gt-amy and glucoamylase.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Parashar D,Satyanarayana T

doi

10.1016/j.ijbiomac.2017.02.083

subject

Has Abstract

pub_date

2017-06-01 00:00:00

pages

274-281

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(16)32807-0

journal_volume

99

pub_type

杂志文章

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