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• W2019291325 abstract "first_page settings Order Article Reprints Font Type: Arial Georgia Verdana Font Size: Aa Aa Aa Line Spacing:    Column Width:    Background: Open AccessCorrection Correction: Yang, C.-H., et al. Immobilization of Brassica oleracea Chlorophyllase 1 (BoCLH1) and Candida rugosa Lipase (CRL) in Magnetic Alginate Beads: An Enzymatic Evaluation in the Corresponding Proteins. Molecules 2014, 19, 11800-11815 by Chih-Hui Yang 1,†, Chih-Chung Yen 1,†, Jyun-Jen Jheng 1, Chih-Yu Wang 2, Sheau-Shyang Chen 1, Pei-Yu Huang 1, Keng-Shiang Huang 3,* and Jei-Fu Shaw 1,* 1 Department of Biological Science & Technology, I-Shou University, Kaohsiung 840, Taiwan 2 Department of Biomedical Engineering, I-Shou University, Kaohsiung 840, Taiwan 3 The School of Chinese Medicine for Post-Baccalaureate, I-Shou University, No. 8, Yida Road, Jiaosu Village Yanchao District, Kaohsiung 82445, Taiwan * Authors to whom correspondence should be addressed. † These authors contributed equally to this work. Molecules 2015, 20(4), 7325-7328; https://doi.org/10.3390/molecules20047325 Received: 2 April 2015 / Accepted: 2 April 2015 / Published: 21 April 2015 (This article belongs to the Special Issue Bio and Nanomaterials Based on Fe3O4) Download Download PDF Download PDF with Cover Download XML Download Epub Browse Figures Versions Notes The authors wish to correct Scheme 1, and Figure 1, Figure 4 and Figure 7 in [1] as follows.Scheme 1 should include phytol and fatty acid. Scheme 1. Enzymatic reaction of Chlorophyllase (CLH) and lipase. (A) Chlorophyllase catalyzes the hydrolysis of chlorophyll a (Chl a), chlorophyllide (Chlide a) and phytol. (B) Lipase catalyzes hydrolysis or synthesis of a triglycerol. Scheme 1. Enzymatic reaction of Chlorophyllase (CLH) and lipase. (A) Chlorophyllase catalyzes the hydrolysis of chlorophyll a (Chl a), chlorophyllide (Chlide a) and phytol. (B) Lipase catalyzes hydrolysis or synthesis of a triglycerol. In Figure 1 Alginate should replace Chitosan: Figure 1. Schematic diagram showing the synthesis of enzyme encapsulated magnetic alginate composite beads. MIO is magnetic iron oxide (Fe3O4 nanoparticles); BoCLH1 is Brassica oleracea chlorophyllase 1; CRL is Candida rugosa lipase. Figure 1. Schematic diagram showing the synthesis of enzyme encapsulated magnetic alginate composite beads. MIO is magnetic iron oxide (Fe3O4 nanoparticles); BoCLH1 is Brassica oleracea chlorophyllase 1; CRL is Candida rugosa lipase. Figure 4A,B should be replaced. The correct Figure 4 is as follows: Figure 4. The degradation of alginate beads in various pH environments. Figure 4. The degradation of alginate beads in various pH environments. In Figure 7 CRL entrapped in the alginate (∆) and MIO NP-alginate (▲) should be labeled: Figure 7. The residual activity of the BoCLH1 in the alginate (□) and MIO NP-alginate (■) and CRL entrapped in the alginate (∆) and MIO NP-alginate (▲) at pH 6 in reaction buffer for 30 min each cycle. Figure 7. The residual activity of the BoCLH1 in the alginate (□) and MIO NP-alginate (■) and CRL entrapped in the alginate (∆) and MIO NP-alginate (▲) at pH 6 in reaction buffer for 30 min each cycle. The authors would like to apologize for any inconvenience caused to the readers by these changes. The article will be updated on the journal website, with the original version remaining available at the same location. ReferenceYang, C.-H.; Yen, C.-C.; Jheng, J.-J.; Wang, C.-Y.; Chen, S.-S.; Huang, P.-Y.; Huang, K.-S.; Shaw, J.-F. Immobilization of Brassica oleracea Chlorophyllase 1 (BoCLH1) and Candida rugosa Lipase (CRL) in Magnetic Alginate Beads: An Enzymatic Evaluation in the Corresponding Proteins. Molecules 2014, 19, 11800–11815. [Google Scholar] [CrossRef] [PubMed] © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/). Share and Cite MDPI and ACS Style Yang, C.-H.; Yen, C.-C.; Jheng, J.-J.; Wang, C.-Y.; Chen, S.-S.; Huang, P.-Y.; Huang, K.-S.; Shaw, J.-F. Correction: Yang, C.-H., et al. Immobilization of Brassica oleracea Chlorophyllase 1 (BoCLH1) and Candida rugosa Lipase (CRL) in Magnetic Alginate Beads: An Enzymatic Evaluation in the Corresponding Proteins. Molecules 2014, 19, 11800-11815. Molecules 2015, 20, 7325-7328. https://doi.org/10.3390/molecules20047325 AMA Style Yang C-H, Yen C-C, Jheng J-J, Wang C-Y, Chen S-S, Huang P-Y, Huang K-S, Shaw J-F. Correction: Yang, C.-H., et al. Immobilization of Brassica oleracea Chlorophyllase 1 (BoCLH1) and Candida rugosa Lipase (CRL) in Magnetic Alginate Beads: An Enzymatic Evaluation in the Corresponding Proteins. Molecules 2014, 19, 11800-11815. Molecules. 2015; 20(4):7325-7328. https://doi.org/10.3390/molecules20047325 Chicago/Turabian Style Yang, Chih-Hui, Chih-Chung Yen, Jyun-Jen Jheng, Chih-Yu Wang, Sheau-Shyang Chen, Pei-Yu Huang, Keng-Shiang Huang, and Jei-Fu Shaw. 2015. Correction: Yang, C.-H., et al. Immobilization of Brassica oleracea Chlorophyllase 1 (BoCLH1) and Candida rugosa Lipase (CRL) in Magnetic Alginate Beads: An Enzymatic Evaluation in the Corresponding Proteins. Molecules 2014, 19, 11800-11815 Molecules 20, no. 4: 7325-7328. https://doi.org/10.3390/molecules20047325 Find Other Styles Article Metrics No No Article Access Statistics For more information on the journal statistics, click here. Multiple requests from the same IP address are counted as one view." @default.
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