The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: β-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: β-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. In spite of catalytic efficiencies of <1 % of the natural reactions, we demonstrate the utility of given phosphorylase-sugar phosphate pairs to access new-to-nature fragments of human milk oligosaccharides, or analogues thereof, in multi-milligram quantities.

中文翻译：

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β-1,4- 和 β-1,3-葡聚糖磷酸化酶的制备和动力学分析为获取人乳寡糖片段及其类似物提供信息。

寡糖的酶促合成取决于合适酶的可用性，这仍然是一个限制。在不求助于酶工程或进化方法的情况下，本文中我们证明了野生型纤维糊精磷酸化酶（CDP：β-1,4-葡聚糖连接依赖性）和昆布糊精磷酸化酶（Pro_7066：β-1,3-葡聚糖连接依赖性）的能力）能够耐受许多糖-1-磷酸底物，尽管动力学效率降低。尽管天然反应的催化效率<1%，我们证明了给定的磷酸化酶-磷酸糖对在获取数毫克量的人乳寡糖或其类似物的新性质片段方面的效用。