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

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 (SBD GA ) or Arabidopsis thaliana glucan, water dikinase 3 (SBD GWD3 ) 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... Mehr ...

Verfasser: Wang, Yu
Tian, Yu
Zhong, Yuyue
Suleiman, Mohammad Amer
Feller, Georges
Westh, Peter
Blennow, Andreas
Møller, Marie Sofie
Svensson, Birte
Dokumenttyp: Artikel
Erscheinungsdatum: 2023
Reihe/Periodikum: 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 , pp. 9040-9050 . https://doi.org/10.1021/acs.jafc.3c01898
Schlagwörter: Carbohydrate-binding module / Waxy starch / Normal starch / High-amylose starch / Pseudoalteromonas haloplanktis α-amylase / Heterogenous catalysis / Sabatier principle
Sprache: Englisch
Permalink: https://search.fid-benelux.de/Record/base-29235910
Datenquelle: BASE; Originalkatalog
Powered By: BASE
Link(s) : https://orbit.dtu.dk/en/publications/7f425908-feb7-495c-9f4d-18ef9b583c4f

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 (SBD GA ) or Arabidopsis thaliana glucan, water dikinase 3 (SBD GWD3 ) 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 SBD GA compared to SBD GWD3 was accompanied by the superior activity of AHA-SBD GA in agreement with the Sabatier principle of adsorption limited heterogenous catalysis.