Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion. / Wang, Yu; Tian, Yu; Zhong, Yuyue; Suleiman, Mohammad Amer; Feller, Georges; Westh, Peter; Blennow, Andreas; Møller, Marie Sofie; Svensson, Birte.

In: Journal of Agricultural and Food Chemistry, Vol. 71, No. 23, 2023, p. 9040-9050.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wang, Y, Tian, Y, Zhong, Y, Suleiman, MA, Feller, G, Westh, P, Blennow, A, Møller, MS & Svensson, B 2023, 'Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion', Journal of Agricultural and Food Chemistry, vol. 71, no. 23, pp. 9040-9050. https://doi.org/10.1021/acs.jafc.3c01898

APA

Wang, Y., Tian, Y., Zhong, Y., Suleiman, M. A., Feller, G., Westh, P., Blennow, A., Møller, M. S., & Svensson, B. (2023). Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion. Journal of Agricultural and Food Chemistry, 71(23), 9040-9050. https://doi.org/10.1021/acs.jafc.3c01898

Vancouver

Wang Y, Tian Y, Zhong Y, Suleiman MA, Feller G, Westh P et al. Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion. Journal of Agricultural and Food Chemistry. 2023;71(23):9040-9050. https://doi.org/10.1021/acs.jafc.3c01898

Author

Wang, Yu ; Tian, Yu ; Zhong, Yuyue ; Suleiman, Mohammad Amer ; Feller, Georges ; Westh, Peter ; Blennow, Andreas ; Møller, Marie Sofie ; Svensson, Birte. / Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion. In: Journal of Agricultural and Food Chemistry. 2023 ; Vol. 71, No. 23. pp. 9040-9050.

Bibtex

@article{9c6bbf22ce6c41119425681b686b2076,
title = "Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion",
abstract = "Degradation of starch granules by a psychrophilic α-amylase, AHA, from the Antarctic bacterium Pseudoalteromonas haloplanktis TAB23 was facilitated by C-terminal fusion to a starch-binding domain (SBD) from either Aspergillus niger glucoamylase (SBDGA) or Arabidopsis thaliana glucan, water dikinase 3 (SBDGWD3) via a decapeptide linker. Depending on the waxy, normal or high-amylose starch type and the botanical source, the AHA-SBD fusion enzymes showed up to 3 times higher activity than AHA wild-type. The SBD-fusion thus increased the density of enzyme attack-sites and binding-sites on the starch granules by up to 5- and 7-fold, respectively, as measured using an interfacial catalysis approach that combined conventional Michaelis-Menten kinetics, with the substrate in excess, and inverse kinetics, having enzyme in excess, with enzyme-starch granule adsorption isotherms. Higher substrate affinity of the SBDGA compared to SBDGWD3 was accompanied by the superior activity of AHA-SBDGA in agreement with the Sabatier principle of adsorption limited heterogenous catalysis.",
keywords = "alpha-Amylases/chemistry, Hydrolysis, Protein Structure, Tertiary, Starch/chemistry, Amylose/chemistry",
author = "Yu Wang and Yu Tian and Yuyue Zhong and Suleiman, {Mohammad Amer} and Georges Feller and Peter Westh and Andreas Blennow and M{\o}ller, {Marie Sofie} and Birte Svensson",
year = "2023",
doi = "10.1021/acs.jafc.3c01898",
language = "English",
volume = "71",
pages = "9040--9050",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "23",

}

RIS

TY - JOUR

T1 - Improved Hydrolysis of Granular Starches by a Psychrophilic α-Amylase Starch Binding Domain-Fusion

AU - Wang, Yu

AU - Tian, Yu

AU - Zhong, Yuyue

AU - Suleiman, Mohammad Amer

AU - Feller, Georges

AU - Westh, Peter

AU - Blennow, Andreas

AU - Møller, Marie Sofie

AU - Svensson, Birte

PY - 2023

Y1 - 2023

N2 - Degradation of starch granules by a psychrophilic α-amylase, AHA, from the Antarctic bacterium Pseudoalteromonas haloplanktis TAB23 was facilitated by C-terminal fusion to a starch-binding domain (SBD) from either Aspergillus niger glucoamylase (SBDGA) or Arabidopsis thaliana glucan, water dikinase 3 (SBDGWD3) via a decapeptide linker. Depending on the waxy, normal or high-amylose starch type and the botanical source, the AHA-SBD fusion enzymes showed up to 3 times higher activity than AHA wild-type. The SBD-fusion thus increased the density of enzyme attack-sites and binding-sites on the starch granules by up to 5- and 7-fold, respectively, as measured using an interfacial catalysis approach that combined conventional Michaelis-Menten kinetics, with the substrate in excess, and inverse kinetics, having enzyme in excess, with enzyme-starch granule adsorption isotherms. Higher substrate affinity of the SBDGA compared to SBDGWD3 was accompanied by the superior activity of AHA-SBDGA in agreement with the Sabatier principle of adsorption limited heterogenous catalysis.

AB - Degradation of starch granules by a psychrophilic α-amylase, AHA, from the Antarctic bacterium Pseudoalteromonas haloplanktis TAB23 was facilitated by C-terminal fusion to a starch-binding domain (SBD) from either Aspergillus niger glucoamylase (SBDGA) or Arabidopsis thaliana glucan, water dikinase 3 (SBDGWD3) via a decapeptide linker. Depending on the waxy, normal or high-amylose starch type and the botanical source, the AHA-SBD fusion enzymes showed up to 3 times higher activity than AHA wild-type. The SBD-fusion thus increased the density of enzyme attack-sites and binding-sites on the starch granules by up to 5- and 7-fold, respectively, as measured using an interfacial catalysis approach that combined conventional Michaelis-Menten kinetics, with the substrate in excess, and inverse kinetics, having enzyme in excess, with enzyme-starch granule adsorption isotherms. Higher substrate affinity of the SBDGA compared to SBDGWD3 was accompanied by the superior activity of AHA-SBDGA in agreement with the Sabatier principle of adsorption limited heterogenous catalysis.

KW - alpha-Amylases/chemistry

KW - Hydrolysis

KW - Protein Structure, Tertiary

KW - Starch/chemistry

KW - Amylose/chemistry

U2 - 10.1021/acs.jafc.3c01898

DO - 10.1021/acs.jafc.3c01898

M3 - Journal article

C2 - 37264600

VL - 71

SP - 9040

EP - 9050

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 23

ER -

ID: 358498322