作者: Wanchai Yenpetch , Kanoktip Packdibamrung , Wolfgang Zimmermann , Piamsook Pongsawasdi
DOI: 10.1007/S12033-010-9337-7
关键词:
摘要: Cyclodextrin glycosyltransferase (CGTase) from Paenibacillus sp. RB01 and its recombinant enzyme exhibit three isoforms (I, II, III) with the same apparent size but different charge. Here, we demonstrate for first time that deamidation of labile Asns causes change in molecular forms CGTase. The faster increase number was observed upon incubation buffer at more alkaline pH. levels isoform II III over correlated isoaspartate, a unique product. predicted were individually mutated to Asp, then selected mutant wild type tryptic digested investigated by MALDI-TOF. From results, Asn427 most susceptible residue deamidation, followed Asn336, Asn415, Asn567. In addition, Gln389 might also share role. advantage using appropriate CGTase cyclodextrin production is reported.