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首页> 外文期刊>Current Science: A Fortnightly Journal of Research >Determination of oxalate in foodstuffs with arylamine glass-bound oxalateoxidase and peroxidase
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Determination of oxalate in foodstuffs with arylamine glass-bound oxalateoxidase and peroxidase

机译：芳胺玻璃结合的草酸氧化酶和过氧化物酶测定食品中的草酸

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In plants, oxalic acid is derived from oxidative breakdown of carbohydrate and protein. Edible plant tissues contain considerable amount of soluble oxalate, some of which forms an insoluble salt with calcium and thus makes the calcium unavailable in the diet. Patients with calcium oxalate urolithiasis are advised by clinicians to avoid an oxalate-rich diet, as high consumption of oxalate leads to a high level of oxalate in plasma, which might deposit in the kidney as insoluble calcium oxalate to form urinary stones. Hence the measurement of oxalate in foodstuffs is very important. Different methods have been used to measure oxalate in foodstuffs such as permanganate titrimetry, colorimetry, capillary electrophoresis, spectrophotometry, GLC, HPLC, isotachophoresis and ion chromatography. Of these methods, the first two are non-specific and less accurate, while the rest require expensive apparatus and trained personnel to operate. Although all enzymatic colorimetric method employing oxalate oxidase and peroxidase is simple, sensitive, and specific and does not require costly equipment9, it becomes expensive for a large number of samples, due to the requirement of bulk quantity of enzyme. Immobilization of enzyme on insoluble support provides its reuse and thus reduces the cost of procedure. Recently, we have reported the immobilization of barley oxalate oxidase onto alkylamine glass beads through glutaraldehyde coupling, for determination of oxalate in a few foodstuff. However, the immobilization of an enzyme on alkylamine glass through glutaraldehyde coupling has the disadvantage of extensive self-polymerization nature of glutaraldehyde and protein crosslinking, and hence the support needs to be washed well prior to enzyme additionTM. Further, the gtutaraldehyde coupling involves Schiff's base formation, which has a drawback of reversibility of the reaction at low pH. These problems were overcome by immobilizing oxalate oxidase and peroxidase onto arylamine glass beads through diazotization. The present report describes the use of arylamine glass-bound enzymes for deterruination of oxalate in various foodstuffs.
机译：在植物中，草酸来源于碳水化合物和蛋白质的氧化分解。食用植物组织中含有大量的可溶性草酸盐，其中一些草酸盐与钙形成了不溶性盐，因此使钙无法从饮食中获取。临床医生建议患有草酸钙尿路结石的患者避免食用富含草酸的饮食，因为草酸的大量摄入会导致血浆中草酸的含量很高，草酸可能以不溶性草酸钙的形式沉积在肾脏中，形成尿结石。因此，食品中草酸盐的测定非常重要。已使用不同的方法测量食品中的草酸盐，例如高锰酸盐滴定法，比色法，毛细管电泳，分光光度法，GLC，HPLC，等速电泳和离子色谱法。在这些方法中，前两种是非特定性的且准确性较低，而其余方法则需要昂贵的设备和训练有素的人员进行操作。尽管所有采用草酸氧化酶和过氧化物酶的酶法比色法都很简单，灵敏，特异，并且不需要昂贵的设备9，但由于需要大量的酶，对于大量样品而言它变得昂贵。将酶固定在不溶性支持物上可以重复使用，从而降低了操作成本。最近，我们报道了通过戊二醛偶联将大麦草酸氧化酶固定在烷基胺玻璃珠上，用于测定几种食品中的草酸。但是，通过戊二醛偶联将酶固定在烷基胺玻璃上的缺点是戊二醛具有广泛的自聚合性质和蛋白质交联性，因此需要在添加酶之前充分洗涤载体。此外，戊二醛偶联涉及席夫碱的形成，其具有在低pH下反应可逆的缺点。通过重氮化将草酸盐氧化酶和过氧化物酶固定在芳胺玻璃珠上可以克服这些问题。本报告描述了使用芳基胺玻璃结合的酶对各种食品中草酸盐的去污作用。

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