TY - JOUR
T1 - Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose
AU - Gangoiti, Joana
AU - Pijning, Tjaard
AU - Dijkhuizen, Lubbert
N1 - Copyright © 2017. Published by Elsevier Inc.
PY - 2018/2
Y1 - 2018/2
N2 - Transglucosidases belonging to the glycoside hydrolase (GH) family 70 are promising enzymatic tools for the synthesis of α-glucans with defined structures from renewable sucrose and starch substrates. Depending on the GH70 enzyme specificity, α-glucans with different structures and physicochemical properties are produced, which have found diverse (potential) commercial applications, e.g. in food, health and as biomaterials. Originally, the GH70 family was established only for glucansucrase enzymes of lactic acid bacteria that catalyze the synthesis of α-glucan polymers from sucrose. In recent years, we have identified 3 novel subfamilies of GH70 enzymes (designated GtfB, GtfC and GtfD), inactive on sucrose but converting starch/maltodextrin substrates into novel α-glucans. These novel starch-acting enzymes considerably enlarge the panel of α-glucans that can be produced. They also represent very interesting evolutionary intermediates between sucrose-acting GH70 glucansucrases and starch-acting GH13 α-amylases. Here we provide an overview of the repertoire of GH70 enzymes currently available with focus on these novel starch-acting GH70 enzymes and their biotechnological potential. Moreover, we discuss key developments in the understanding of structure-function relationships of GH70 enzymes in the light of available three-dimensional structure structures, and the protein engineering strategies that were recently applied to expand their natural product specificities.
AB - Transglucosidases belonging to the glycoside hydrolase (GH) family 70 are promising enzymatic tools for the synthesis of α-glucans with defined structures from renewable sucrose and starch substrates. Depending on the GH70 enzyme specificity, α-glucans with different structures and physicochemical properties are produced, which have found diverse (potential) commercial applications, e.g. in food, health and as biomaterials. Originally, the GH70 family was established only for glucansucrase enzymes of lactic acid bacteria that catalyze the synthesis of α-glucan polymers from sucrose. In recent years, we have identified 3 novel subfamilies of GH70 enzymes (designated GtfB, GtfC and GtfD), inactive on sucrose but converting starch/maltodextrin substrates into novel α-glucans. These novel starch-acting enzymes considerably enlarge the panel of α-glucans that can be produced. They also represent very interesting evolutionary intermediates between sucrose-acting GH70 glucansucrases and starch-acting GH13 α-amylases. Here we provide an overview of the repertoire of GH70 enzymes currently available with focus on these novel starch-acting GH70 enzymes and their biotechnological potential. Moreover, we discuss key developments in the understanding of structure-function relationships of GH70 enzymes in the light of available three-dimensional structure structures, and the protein engineering strategies that were recently applied to expand their natural product specificities.
KW - GH70
KW - Glucansucrase
KW - Glucanotransferase
KW - alpha-glucan
KW - lactic acid bacteria
KW - structure-function
KW - 4,6-ALPHA-GLUCANOTRANSFERASE ENZYMES
KW - BRANCHING SUCRASE
KW - LACTOBACILLUS-REUTERI 180
KW - MESENTEROIDES NRRL B-1299
KW - LACTIC-ACID BACTERIA
KW - STREPTOCOCCUS-MUTANS GLUCOSYLTRANSFERASES
KW - 2 CATALYTIC DOMAINS
KW - LEUCONOSTOC-MESENTEROIDES
KW - MOLECULAR CHARACTERIZATION
KW - STRUCTURAL-ANALYSIS
U2 - 10.1016/j.biotechadv.2017.11.001
DO - 10.1016/j.biotechadv.2017.11.001
M3 - Review article
C2 - 29133008
SN - 0734-9750
VL - 36
SP - 196
EP - 207
JO - Biotechnology Advances
JF - Biotechnology Advances
ER -