Extensive hydrolysis of raw rice starch by a chimeric α-amylase engineered with α-amylase (AmyP) and a starch-binding domain from Cryptococcus sp. S-2

Peng, Hui; Li, Rui; Li, Fengling; Zhai, Lu; Zhang, Xiaohan; Xiao, Yazhong; Gao, Yin

doi:10.1007/s00253-017-8638-1

Cited by 14 publications

(14 citation statements)

References 40 publications

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“…Due to lack of data of other raw microalgae starch, the hydrolysis efficiency is compared with that of raw rice starch. AmyP is known to preferentially finish the hydrolysis of raw rice starch in 4 h, leading to approximately 15% hydrolysis for 10% raw starch, which is unaffected by CaCl 2 . Thus, AmyP is more efficient in raw microalgae starch than in raw rice starch.…”

Section: Discussionmentioning

confidence: 99%

“…When hydrolysis curves of raw microalgae starch were determined, two starch concentrations were used, 4% and 8%. The degradation of granular starch was performed according to Peng et al 28 Briefly, AmyP and PPA were used at their pH and temperature optima (25 mM Bis-tris buffer, pH 7.5 for both AmyP and PPA; 40 °C for AmyP; 37 °C for PPA). The effect of calcium ion was tested by adding 5 mM CaCl 2 to the reaction mixture.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Efficient Hydrolysis of Raw Microalgae Starch by an α-Amylase (AmyP) of Glycoside Hydrolase Subfamily GH13_37

Peng

Zhai

Suo

et al. 2018

J. Agric. Food Chem.

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Microalgae starch is receiving increasing attention as a renewable feedstock for biofuel production. Raw microalgae starch from Tetraselmis subcordiformis was proven to be very efficiently hydrolyzed by an α-amylase (AmyP) of glycoside hydrolase subfamily GH13_37 below the temperature of gelatinization (40 °C). The hydrolysis degree reached 74.4 ± 2.2% for 4% raw microalgae starch and 53.2 ± 1.7% for 8% raw microalgae starch after only 2 h. The hydrolysis efficiency was significantly stimulated by calcium ions. The enzyme catalysis of AmyP and its mutants (Q306A and E347A) suggested that calcium ions contributed to the hydrolysis of cyclic structures in raw microalgae starch by a distinctive calcium-binding site Ca2 of AmyP. The study explored raw microalgae starch as a new resource for cold enzymatic hydrolysis and extended our knowledge on the function of calcium in amylolytic enzyme.

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Section: Discussionmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Efficient Hydrolysis of Raw Microalgae Starch by an α-Amylase (AmyP) of Glycoside Hydrolase Subfamily GH13_37

Peng

Zhai

Suo

et al. 2018

J. Agric. Food Chem.

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“…For efficient hydrolysis of the starch molecule, gelatinization and liquefaction often precede saccharification, incurring a high cost of production and other difficulties [ 3 ]. Utilizing native/raw starch hydrolyzing amylases for starch liquefaction and saccharification saves time and cost of heating while increasing process efficiency [ 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Nwagu

Aoyagi

Okolo

et al. 2020

Heliyon

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Amylase capable of raw starch digestion presents a cheap and easier means of reducing sugar generation from various starch sources. Unfortunately, its potential for use in numerous industrial processes is hindered by poor stability. In this work, chemical modification by acylation using citraconic anhydride (CA) and maleic anhydride (MA) was used to stabilize the raw starch saccharifying amylase from A. carbonarius . The effect of the anhydrides on the pH and thermal stability of the free amylase was investigated. Enzyme kinetics and thermodynamic studies of the free and modified amylase were also carried out. Blue shifts in fluorescent spectra were observed after modification with both anhydrides. Citraconylation led to increased affinity of the enzyme for raw potato starch, unlike maleylation. The activation energy (kJ mol −1 ) for enzyme inactivation was increased by 94.8% after modification with CA while only 17.9% increase was noted after modification with MA. Acylation led to an increase in Gibb's free energy and enthalpy while a reduction in entropy was observed. At 80 °C the half-life (h) was 5.92, 11.18 and 14.74 for free, MA and CA enzyme samples, respectively. These findings have potential value in all industries interested in starch conversion to sugars.

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“…On the other hand, the addition of CBM20 in the α-amylase from Cryptococcus sp. S-2 enhanced the catalytic efficiency and thermostability of α-amylase (AmyP) toward raw rice starch [50].…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of Recombinant Raw Starch Degrading α-Amylase from Roseateles terrae HL11 and Its Application on Cassava Pulp Saccharification

et al. 2022

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Exploring new raw starch-hydrolyzing -amylases and understanding their biochemical characteristics are important for the utilization of starch-rich materials in bio-industry. In this work, the biochemical characteristics of a novel raw starch-degrading -amylase (HL11 Amy) from Roseateles terrae HL11 was firstly reported. Evolutionary analysis revealed that HL11Amy was classified into glycoside hydrolase family 13 subfamily 32 (GH13_32). It contains four protein domains consisting of domain A, domain B, domain C and carbohydrate-binding module 20 (CMB20). The enzyme optimally worked at 50 °C, pH 4.0 with a specific activity of 6270 U/mg protein and 1030 raw starch-degrading (RSD) U/mg protein against soluble starch. Remarkably, HL11Amy exhibited activity toward both raw and gelatinized forms of various substrates, with the highest catalytic efficiency (kcat/Km) on starch from rice, followed by potato and cassava, respectively. HL11Amy effectively hydrolyzed cassava pulp (CP) hydrolysis, with a reducing sugar yield of 736 and 183 mg/g starch from gelatinized and raw CP, equivalent to 72% and 18% conversion based on starch content in the substrate, respectively. These demonstrated that HL11Amy represents a promising raw starch-degrading enzyme with potential applications in starch modification and cassava pulp saccharification.

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Extensive hydrolysis of raw rice starch by a chimeric α-amylase engineered with α-amylase (AmyP) and a starch-binding domain from Cryptococcus sp. S-2

Cited by 14 publications

References 40 publications

Efficient Hydrolysis of Raw Microalgae Starch by an α-Amylase (AmyP) of Glycoside Hydrolase Subfamily GH13_37

Efficient Hydrolysis of Raw Microalgae Starch by an α-Amylase (AmyP) of Glycoside Hydrolase Subfamily GH13_37

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Functional Characterization of Recombinant Raw Starch Degrading α-Amylase from Roseateles terrae HL11 and Its Application on Cassava Pulp Saccharification

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