Identification of a novel starch-converting GtfB enzyme from the Fructilactobacillus sanfranciscensis TMW11304 to reduce the viscoelasticity and retrogradation of tapioca starch
Copyright © 2024 Elsevier B.V. All rights reserved..
Starch-converting α-glucanotransferases are efficient enzymatic toolkits for the biosynthesis of diverse α-glucans, which hold vast application potential in the food industry. In this work, we identified a novel GtfB protein from Fructilactobacillus sanfranciscensis TMW11304 (FsTMW11304 GtfB) in NCBI. Although this enzyme was highly conserved in motifs I-IV with those isomalto-maltopolysaccharides (IMMPs)-producing GtfB α-glucanotransferases, it possessed distinct deletions and mutations in two crucial loops shaping the active site. Hence, unlike those GtfB enzymes, FsTMW11304 GtfB not only exhibited excellent 4,6-α-glucanotransferase activity on amylose to generate atypically low-molecular-weight IMMPs with consecutive linear (α1 → 6) linkages up to 48 %, but also held good capability towards branched substrates. Besides, compared with the control, the treatment by FsTMW11304 GtfB reduced the storage/loss modulus of granular and gelatinized tapioca starches (TS) by 12.0 %/17.9 % and 91.4 %/82.9 %, respectively, indicating that the rigidity of the gel structure was attenuated to different degrees in the two reaction systems. Furthermore, the setback viscosity observed in the gelatinized TS modified by FsTMW11304 GtfB was only 5 % of that observed in the control group, suggesting the short-term anti-retrogradation property has been substantially improved. Thus, FsTMW11304 GtfB represents a meaningful addition to the α-glucanotransferases in GH70 family, which expands the repertoire of diverse α-glucans synthesized from starch and facilitates the understanding of the structure-function relationship of the GtfB α-glucanotransferases.
Medienart: |
E-Artikel |
---|
Erscheinungsjahr: |
2024 |
---|---|
Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:263 |
---|---|
Enthalten in: |
International journal of biological macromolecules - 263(2024), Pt 2 vom: 25. März, Seite 130308 |
Sprache: |
Englisch |
---|
Beteiligte Personen: |
Dong, Jingjing [VerfasserIn] |
---|
Links: |
---|
Themen: |
4,6-Glucanotransferase |
---|
Anmerkungen: |
Date Completed 27.03.2024 Date Revised 27.03.2024 published: Print-Electronic Citation Status MEDLINE |
---|
doi: |
10.1016/j.ijbiomac.2024.130308 |
---|
funding: |
|
---|---|
Förderinstitution / Projekttitel: |
|
PPN (Katalog-ID): |
NLM368915611 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | NLM368915611 | ||
003 | DE-627 | ||
005 | 20240327235915.0 | ||
007 | cr uuu---uuuuu | ||
008 | 240229s2024 xx |||||o 00| ||eng c | ||
024 | 7 | |a 10.1016/j.ijbiomac.2024.130308 |2 doi | |
028 | 5 | 2 | |a pubmed24n1351.xml |
035 | |a (DE-627)NLM368915611 | ||
035 | |a (NLM)38401578 | ||
035 | |a (PII)S0141-8130(24)01111-5 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
100 | 1 | |a Dong, Jingjing |e verfasserin |4 aut | |
245 | 1 | 0 | |a Identification of a novel starch-converting GtfB enzyme from the Fructilactobacillus sanfranciscensis TMW11304 to reduce the viscoelasticity and retrogradation of tapioca starch |
264 | 1 | |c 2024 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ƒaComputermedien |b c |2 rdamedia | ||
338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
500 | |a Date Completed 27.03.2024 | ||
500 | |a Date Revised 27.03.2024 | ||
500 | |a published: Print-Electronic | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
520 | |a Starch-converting α-glucanotransferases are efficient enzymatic toolkits for the biosynthesis of diverse α-glucans, which hold vast application potential in the food industry. In this work, we identified a novel GtfB protein from Fructilactobacillus sanfranciscensis TMW11304 (FsTMW11304 GtfB) in NCBI. Although this enzyme was highly conserved in motifs I-IV with those isomalto-maltopolysaccharides (IMMPs)-producing GtfB α-glucanotransferases, it possessed distinct deletions and mutations in two crucial loops shaping the active site. Hence, unlike those GtfB enzymes, FsTMW11304 GtfB not only exhibited excellent 4,6-α-glucanotransferase activity on amylose to generate atypically low-molecular-weight IMMPs with consecutive linear (α1 → 6) linkages up to 48 %, but also held good capability towards branched substrates. Besides, compared with the control, the treatment by FsTMW11304 GtfB reduced the storage/loss modulus of granular and gelatinized tapioca starches (TS) by 12.0 %/17.9 % and 91.4 %/82.9 %, respectively, indicating that the rigidity of the gel structure was attenuated to different degrees in the two reaction systems. Furthermore, the setback viscosity observed in the gelatinized TS modified by FsTMW11304 GtfB was only 5 % of that observed in the control group, suggesting the short-term anti-retrogradation property has been substantially improved. Thus, FsTMW11304 GtfB represents a meaningful addition to the α-glucanotransferases in GH70 family, which expands the repertoire of diverse α-glucans synthesized from starch and facilitates the understanding of the structure-function relationship of the GtfB α-glucanotransferases | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a 4,6-Glucanotransferase | |
650 | 4 | |a GtfB | |
650 | 4 | |a Pasting properties | |
650 | 4 | |a Rheological properties | |
650 | 4 | |a Starch | |
650 | 7 | |a Starch |2 NLM | |
650 | 7 | |a 9005-25-8 |2 NLM | |
650 | 7 | |a Glucans |2 NLM | |
650 | 7 | |a Amylose |2 NLM | |
650 | 7 | |a 9005-82-7 |2 NLM | |
700 | 1 | |a Bai, Yuxiang |e verfasserin |4 aut | |
700 | 1 | |a Chen, Ying |e verfasserin |4 aut | |
700 | 1 | |a Li, Xiaoxiao |e verfasserin |4 aut | |
700 | 1 | |a Wang, Yanli |e verfasserin |4 aut | |
700 | 1 | |a Fan, Rui |e verfasserin |4 aut | |
700 | 1 | |a Wang, Nana |e verfasserin |4 aut | |
700 | 1 | |a Jin, Zhengyu |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t International journal of biological macromolecules |d 1992 |g 263(2024), Pt 2 vom: 25. März, Seite 130308 |w (DE-627)NLM012627356 |x 1879-0003 |7 nnns |
773 | 1 | 8 | |g volume:263 |g year:2024 |g number:Pt 2 |g day:25 |g month:03 |g pages:130308 |
856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.ijbiomac.2024.130308 |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a GBV_NLM | ||
951 | |a AR | ||
952 | |d 263 |j 2024 |e Pt 2 |b 25 |c 03 |h 130308 |