Journal
CATALYSTS
Volume 12, Issue 6, Pages -Publisher
MDPI
DOI: 10.3390/catal12060647
Keywords
amylase; raw starch; saccharification; biorefinery; cassava pulp
Categories
Funding
- Thailand Graduate Institute of Science and Technology (TGIST) [SCA-CO-2563-12209-TH]
- National Science and Technology Development Agency
- Thammasat University Research Fund
- TUFT [042/2563]
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This study reports a novel raw starch-degrading alpha-amylase (HL11 Amy) from Roseateles terrae HL11, which exhibits potential for applications in starch modification and cassava pulp saccharification.
Exploring new raw starch-hydrolyzing alpha-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 alpha-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 degrees 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 (k(cat)/K-m) 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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