{"title":"喷雾干燥固定化金黄色葡萄球菌脂肪酶(HA25)在洗涤剂行业中的应用","authors":"Hayrunnisa Nadaroglu, Alper Baran, Hatice Bayrakceken","doi":"10.1002/jsde.12784","DOIUrl":null,"url":null,"abstract":"This study aims to produce an active lipase detergent additive dry powder using spray drying. <jats:italic>Staphylococcus aureus</jats:italic> HA25, growing at a pH range of 5.0–8.5, was isolated from Erzurum gogermis cheese and purified using a three‐phase partitioning technique. Optimal immobilization processing conditions were determined for 0.1% wt/wt chitosan, alginate, and chitosan/alginate concentrations of pure lipase enzyme. Morphological features of the immobilized enzyme structure were determined using scanning electron microscopy (SEM) analysis, and structural characterizations were determined using x‐ray diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy, and thermogravimetric (TG) analysis. The results showed that the natural structure of the lipase was largely restored upon reconstitution of the spray‐dried immobilized lipase structures in water. While the free enzyme removed 52.6% of the oil added to the cotton fabric, the immobilized lipase@alginate enzyme removed ~98% of the oil added to the cotton fabric at the highest rate when used as a detergent additive. It was found that the reusability activity of chitosan@lipase, alginate@lipase, and chitosan/alginate@lipase enzymes remained at 86.4%, 92.8%, and 88.6% of their original activity, respectively. The study suggests that immobilized variations of the lipase enzyme within chitosan, alginate, and chitosan/alginate matrices may serve as a natural, secure, and efficient substitute for conventional chemical detergents, offering a non‐toxic alternative for additive materials.","PeriodicalId":17083,"journal":{"name":"Journal of Surfactants and Detergents","volume":null,"pages":null},"PeriodicalIF":1.6000,"publicationDate":"2024-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Spray‐dried immobilized lipase from Staphylococcus aureusHA25 for application in detergent industry\",\"authors\":\"Hayrunnisa Nadaroglu, Alper Baran, Hatice Bayrakceken\",\"doi\":\"10.1002/jsde.12784\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"This study aims to produce an active lipase detergent additive dry powder using spray drying. <jats:italic>Staphylococcus aureus</jats:italic> HA25, growing at a pH range of 5.0–8.5, was isolated from Erzurum gogermis cheese and purified using a three‐phase partitioning technique. Optimal immobilization processing conditions were determined for 0.1% wt/wt chitosan, alginate, and chitosan/alginate concentrations of pure lipase enzyme. Morphological features of the immobilized enzyme structure were determined using scanning electron microscopy (SEM) analysis, and structural characterizations were determined using x‐ray diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy, and thermogravimetric (TG) analysis. The results showed that the natural structure of the lipase was largely restored upon reconstitution of the spray‐dried immobilized lipase structures in water. While the free enzyme removed 52.6% of the oil added to the cotton fabric, the immobilized lipase@alginate enzyme removed ~98% of the oil added to the cotton fabric at the highest rate when used as a detergent additive. It was found that the reusability activity of chitosan@lipase, alginate@lipase, and chitosan/alginate@lipase enzymes remained at 86.4%, 92.8%, and 88.6% of their original activity, respectively. The study suggests that immobilized variations of the lipase enzyme within chitosan, alginate, and chitosan/alginate matrices may serve as a natural, secure, and efficient substitute for conventional chemical detergents, offering a non‐toxic alternative for additive materials.\",\"PeriodicalId\":17083,\"journal\":{\"name\":\"Journal of Surfactants and Detergents\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.6000,\"publicationDate\":\"2024-06-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Surfactants and Detergents\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1002/jsde.12784\",\"RegionNum\":4,\"RegionCategory\":\"工程技术\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Surfactants and Detergents","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1002/jsde.12784","RegionNum":4,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
摘要
本研究旨在利用喷雾干燥法生产一种活性脂肪酶洗涤添加剂干粉。研究人员从 Erzurum gogermis 奶酪中分离出在 pH 值为 5.0-8.5 的条件下生长的金黄色葡萄球菌 HA25,并采用三相分配技术对其进行纯化。确定了纯脂肪酶浓度为 0.1% wt/wt 的壳聚糖、海藻酸和壳聚糖/海藻酸的最佳固定化处理条件。利用扫描电子显微镜(SEM)分析确定了固定化酶结构的形态特征,并利用 X 射线衍射(XRD)、傅立叶变换红外光谱(FTIR)和热重(TG)分析确定了结构特征。结果表明,喷雾干燥固定化脂肪酶结构在水中重组后,脂肪酶的天然结构得到了很大程度的恢复。游离酶对棉织物中油脂的去除率为 52.6%,而固定化脂肪酶@海藻酸盐酶作为洗涤剂添加剂使用时,对棉织物中油脂的去除率高达 98%。研究发现,壳聚糖@脂肪酶、海藻酸@脂肪酶和壳聚糖/海藻酸@脂肪酶的重复使用活性分别保持在其原始活性的 86.4%、92.8% 和 88.6%。研究表明,壳聚糖、海藻酸盐和壳聚糖/海藻酸盐基质中的固定化脂肪酶变体可作为传统化学洗涤剂的天然、安全和高效替代品,为添加剂材料提供了一种无毒替代品。
Spray‐dried immobilized lipase from Staphylococcus aureusHA25 for application in detergent industry
This study aims to produce an active lipase detergent additive dry powder using spray drying. Staphylococcus aureus HA25, growing at a pH range of 5.0–8.5, was isolated from Erzurum gogermis cheese and purified using a three‐phase partitioning technique. Optimal immobilization processing conditions were determined for 0.1% wt/wt chitosan, alginate, and chitosan/alginate concentrations of pure lipase enzyme. Morphological features of the immobilized enzyme structure were determined using scanning electron microscopy (SEM) analysis, and structural characterizations were determined using x‐ray diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy, and thermogravimetric (TG) analysis. The results showed that the natural structure of the lipase was largely restored upon reconstitution of the spray‐dried immobilized lipase structures in water. While the free enzyme removed 52.6% of the oil added to the cotton fabric, the immobilized lipase@alginate enzyme removed ~98% of the oil added to the cotton fabric at the highest rate when used as a detergent additive. It was found that the reusability activity of chitosan@lipase, alginate@lipase, and chitosan/alginate@lipase enzymes remained at 86.4%, 92.8%, and 88.6% of their original activity, respectively. The study suggests that immobilized variations of the lipase enzyme within chitosan, alginate, and chitosan/alginate matrices may serve as a natural, secure, and efficient substitute for conventional chemical detergents, offering a non‐toxic alternative for additive materials.
期刊介绍:
Journal of Surfactants and Detergents, a journal of the American Oil Chemists’ Society (AOCS) publishes scientific contributions in the surfactants and detergents area. This includes the basic and applied science of petrochemical and oleochemical surfactants, the development and performance of surfactants in all applications, as well as the development and manufacture of detergent ingredients and their formulation into finished products.