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
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DOI：
10.1021/acs.jafc.8b03524
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发表时间：
2018-12-05
影响因子：
6.1
通讯作者：
Gao, Yi
中科院分区：
文献类型：
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作者：
Peng, Hui;Zhai, Lu;Gao, Yi
微藻淀粉作为生物燃料生产的可再生原料正受到越来越多的关注。来自亚心形四藻（Tetraselmis subcordiformis）的原始微藻淀粉被证明在低于糊化温度（40 ° C）下被糖苷水解酶亚家族GH13_37的α-淀粉酶（AmyP）非常有效地水解。4%的原微藻淀粉在2 h后水解度达到74.4 ± 2.2%，8%的原微藻淀粉在2 h后水解度达到53.2 ± 1.7%。钙离子对水解效率有显著的促进作用。AmyP及其突变体（Q306 A和E347 A）的酶催化表明，钙离子通过AmyP的独特的钙结合位点Ca 2促进了原微藻淀粉中环状结构的水解。本研究探索了微藻原淀粉作为冷酶解新资源的可能性，并进一步加深了对钙在淀粉酶解中作用的认识。
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 alpha-amylase (AmyP) of glycoside hydrolase subfamily GH13_37 below the temperature of gelatinization (40 degrees 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.