Characterization of β-N-acetylglucosaminidase from a marine Pseudoalteromonas sp. for application in N-acetyl-glucosamine production

H. Park, J. Yim, Hyunro Park, Dockyu Kim
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引用次数: 6

Abstract

ABSTRACT The psychrotolerant Pseudoalteromonas issachenkonii PAMC 22718 was isolated for its high exo-acting chitinase activity in the Kara Sea, Arctic. An exo-acting chitinase (W-Chi22718) was homogeneously purified from the culture supernatant of PAMC 22718, the molecular weight of which was estimated to be approximately 112 kDa. Due to its β-N-acetylglucosaminidase activity, W-Chi22718 was able to produce N-acetyl-D-glucosamine (GlcNAc) monomers from chitin oligosaccharide substrates. W-Chi22718 displayed chitinase activity from 0 to 37°C (optimal temperature of 30°C) and maintained activity from pH 6.0 to 9.0 (optimal pH of 7.6). W-Chi22718 exhibited a relative activity of 13 and 35% of maximal activity at 0 and 10°C, respectively, which is comparable to the activities of previously characterized, cold-adapted bacterial chitinases. W-Chi22718 activity was enhanced by K+, Ca2+, and Fe2+, but completely inhibited by Cu2+ and SDS. We found that W-Chi22718 can produce much more (GlcNAcs) from colloidal chitin, working together with previously characterized cold-active endochitinase W-Chi21702. Genome sequencing revealed that the corresponding gene (chi22718_IV) was 2,856 bp encoding a 951 amino acid protein with a calculated molecular weight of approximately 102 kDa.
海洋假交替单胞菌sp. β- n -乙酰氨基葡萄糖酶在n -乙酰氨基葡萄糖生产中的应用
摘要/ ABSTRACT摘要:从北极喀拉海分离到耐寒异变假单胞菌issachenkonii PAMC 22718,其外显作用几丁质酶活性高。从PAMC 22718的培养上清中均质纯化出一种外显作用几丁质酶(W-Chi22718),估计其分子量约为112 kDa。由于其β- n -乙酰氨基葡萄糖酶活性,W-Chi22718能够从几丁质低聚糖底物中产生n -乙酰- d -氨基葡萄糖(GlcNAc)单体。W-Chi22718在0 ~ 37°C(最适温度为30°C)范围内显示几丁质酶活性,在pH 6.0 ~ 9.0(最适pH 7.6)范围内保持活性。W-Chi22718在0°C和10°C时的相对活性分别为最大活性的13%和35%,这与先前表征的冷适应细菌几丁质酶的活性相当。W-Chi22718活性在K+、Ca2+和Fe2+作用下增强,在Cu2+和SDS作用下完全被抑制。我们发现W-Chi22718可以从胶体几丁质中产生更多(GlcNAcs),与先前表征的冷活性几丁质内切酶W-Chi21702一起工作。基因组测序结果显示,对应基因chi22718_IV全长2856 bp,编码951个氨基酸的蛋白,计算分子量约为102 kDa。
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