Polymer Materials Research Department, Advanced Technologies and New Material Research Institute, Mubarak City for Scientific Research and Technology Applications, New Borg El-Arab City, Alexandria, Egypt.
Appl Biochem Biotechnol. 2011 May;164(1):10-22. doi: 10.1007/s12010-010-9110-1. Epub 2010 Nov 1.
ρ-Benzoquinone-activated alginate beads were presented as a new carrier for affinity covalent immobilization of glucoamylase enzyme. Evidences of alginate modification were extracted from FT-IR and thermal gravimetric analysis and supported by morphological changes recognized through SEM examination. Factors affecting the modification process such as ρ-benzoquinone (PBQ) concentration, reaction time, reaction temperature, reaction pH and finally alginate concentration, have been studied. Its influence on the amount of coupled PBQ was consequently correlated to the changes of the catalytic activity and the retained activity of immobilized enzyme, the main parameters judging the success of the immobilization process. The immobilized glucoamylase was found kept almost 80% of its native activity giving proof of non-significant substrate, starch, diffusion limitation. The proposed affinity covalent immobilizing technique would rank among the potential strategies for efficient immobilization of glucoamylase enzyme.
ρ-苯醌活化的海藻酸钠珠粒被提出作为一种新的亲和共价固定化葡萄糖淀粉酶的载体。从傅里叶变换红外光谱和热重分析中提取了海藻酸钠修饰的证据，并通过 SEM 检查识别的形态变化得到支持。研究了影响修饰过程的因素，如 ρ-苯醌 (PBQ) 浓度、反应时间、反应温度、反应 pH 值，最后是海藻酸钠浓度。其对耦合 PBQ 量的影响与固定化酶的催化活性和保留活性的变化相关，这些是判断固定化过程成功的主要参数。固定化葡萄糖淀粉酶的活性保持在其天然活性的近 80%，这证明了没有明显的底物、淀粉、扩散限制。所提出的亲和共价固定化技术将成为葡萄糖淀粉酶酶有效固定化的潜在策略之一。
