ANEXO I: This readme.txt file was generated on 2022-04-14 by Saul Vallejos Calzada GENERAL INFORMATION 1. Title of dataset: Dataset of the work "Film-shaped reusable smart polymer to produce lactose-free milk by simple immersion" 2. Autorship Name: Jorge Lucas Vallejo García Institution: Departamento de Química. Universidad de Burgos Email: jlvallejo@ubu.es ORCID: https://orcid.org/0000-0002-4586-6102 Name: Ana Arnaiz Alonso Institution: Departamento de Química. Universidad de Burgos Email: anaaa@ubu.es ORCID: https://orcid.org/0000-0002-3842-498X Name: María Dolores Busto Nuñez Institution: Departamento de Biotecnología y Ciencia de los Alimentos. Universidad de Burgos Email: dbusto@ubu.es ORCID: https://orcid.org/0000-0003-1647-7850 Name: José Miguel García Pérez Institution: Departamento de Química. Universidad de Burgos Email: jmiguel@ubu.es ORCID: https://orcid.org/0000-0002-2674-8194 Name: Saul Vallejos Calzada Institution: Departamento de Química. Universidad de Burgos Email: svallejos@ubu.es ORCID: https://orcid.org/0000-0001-5522-6574 DESCRIPTION ----------- 1. Dataset language English 2. Abstract: The dataset contains all raw data of the work "Film-shaped reusable smart polymer to produce lactose-free milk by simple immersion" 3. Keywords: -galactosidase; lactose-free; low-lactose; lactose hydrolysis; enzyme inmobilization. 4. Date of data collection 2022-2023 5. Date of dataset publication 2022-04-17 6. Funding We gratefully acknowledge the financial support provided by all funders. This work was supported by the Regional Government of Castilla y León (Junta de Castilla y León) and by the Ministry of Science and Innovation MICIN and the European Union NextGenerationEU PRTR. Author J. M. García received grant PID2020-113264RB-I00 funded by MCIN/AEI/ 10.13039/501100011033 and by “ERDF A way of making Europe”. A. Arnaiz received funding from Ministerio de Universidades-European Union in the frame of NextGenerationEU RD 289/2021 (Universidad Politécnica de Madrid). J. L. Vallejo-García received the grant PRE2021-09812 funded by MCIN/AEI/ 10.13039/501100011033 and by “ESF Investing in your future”. 7. Geographic location/s of data collection Burgos (Spain) ACCESS INFORMATION ------------------ 1. Dataset Creative Commons License: CC 4.0 Internacional 2. Dataset DOI: XXXXXXXXXXXXXXXXXXX 3. Related publication The related article has been sent to: Materials Today METHODOLOGICAL INFORMATION -------------------------- The polymers thermal characterization was performed by thermogravimetric analysis (Q50 TGA analyzer, TA Instruments, New Castle, DE, USA) with 10–15 mg of sample under synthetic air and nitrogen atmosphere at 10°C·min−1. Infrared spectra (FTIR) were recorded with an infrared spectrometer (FT/IR-4200, Jasco, Tokyo, Japan) with an ATR-PRO410-S single reflection accessory. RAMAN spectra were recorded with a confocal AFM-RAMAN model Alpha300R – Alpha300A AFM from WITec, using a laser radiation of 785 nm, at magnifications of 100x, 12 mW, 10 accumulations. All spectra were taken at room temperature. Enzymatic activity assays were performed using a Synergy HT microplate reader (BioTek®, Winooski, Vermont, USA), recording absorbance data at 420 nm. Digital photographs were taken with a smartphone (Mi 9, Xiaomi, Pekín, China) Field Emission Scanning electron microscopy (FESEM) was carried out using a model GemminiSEM560, ZEISS. Films were dried, freeze fractured, and gold coated in vacuum to ensure the electrical conductivity of the films. The weight percentage of water taken up by the films upon soaking in pure water at 20 ºC until reaching equilibrium (water-swelling percentage, WSP) was obtained from the weight of a dry sample film (ωd) and its water-swelled weight (ωs) using the following expression: WSP = 100×[(ωs×ωd)/ωd]. Film-shaped polymers were prepared by bulk radical polymerization of the commercially available monomers VP (45 mol%), MMA (45 mol%), and SNH2 (10 mol%), the polymeric was crosslinked using 0.1 mol% of E, following the experimental procedure described below. 850 mg (7.64 × 10-3 mol) of VP, 765 mg (7.64 × 10-3 mol) of MMA, 202.5 mg (1.70 × 10-3 mol) of SNH2, 3.4 mg (1.70 × 10-5 mol) of E were mixed. Then, 18.2 mg (1.1 × 10-4 mol) of AIBN were dissolved and the solution of comonomers and initiatior were injected in a mold (90×120×0.1 mm, width, length, thickness) comprised between two silanized glasses in an oxygen-free atmosphere. The polymerization was carried out at 60 °C, overnight, and finally, the films (FNH2) were washed with water. Afterwards, films were washed with water:acetone mixtures ranging from 100:0 to 0:100, and finally with mixtures 0:100 to 100:0. After the preparation of FNH2, 3 solid phase reactions were carried out: (1) generation of benzene diazonium salts on the amino groups provided by the SNH2 monomer (FN2+), (2) immobilization of the enzyme -gal through the formation of diazo bonds (F-gal), and (3) quenching of the leftover benzene diazonium groups with sodium azide (F-gal-N3). Enzymatic activity of F-gal-N3 films were confirmed using ONPG as substrate in a microplate reader with 96-well plates. 6 mm diameter discs were placed at the bottom of each well and 80 L of a citrate-phosphate pH 5 buffer (di-Sodium hydrogen phosphate 0.2 M and citric acid 0.1 M) and 20 L of ONPG substrate at a final concentration of 2.5 mM were added. Samples were incubated for 30 minutes at 37 ºC and the reaction was stopped by adding 100 L of sodium carbonate 10% (w/v). The absorbance of the supernatant was measured at 420 nm, and the enzymatic activity was represented as µmol of ONP/hּ cm2. Following the same experimental procedure, different experiments were carried out to confirm that the polymeric support was inert, that is, that the material without enzyme (FSNH2, FN2+ and FN3) did not show activity. In the same way, a film with deposited enzyme (not immobilized, without covalent anchorage) was also tested and labeled as FAds, which for practical purposes, behaved like a film without enzyme since the successive washes after the deposition process eliminated any enzyme content, making clear the need to carry out a covalent anchorage. Protein release study was carried out with covalently anchored enzyme-containing films to verify that the enzyme is not liberated from the films in aqueous solution. For that, 10 F-gal-N3 discs (6 mm diameter) were incubated for 30 h in citrate-phosphate pH 6.8 buffer (UHT milk's usual pH). 40 µl of samples were taken at different time points (30 minutes, 1, 6, 20 and 30 h), and total protein content was measured according to the method of Bradford. All assays were carried out in triplicate and blanks were used to account for spontaneous breakdown of the substrates. FILE OVERVIEW -------------- FT-IR_Fb-gal.txt FT-IR_Fb-gal-N3.txt FT-IR_FN2+.txt FT-IR_FNH2.txt POC LACTOSE HYDROLYSIS-Figure 5a.ods POC Reutilization-Figure 5b.ods RAMAN_Fb-gal-N3.txt RAMAN_FN2+.txt RAMAN_FNH2.txt RAMAN_Fb-gal.txt TGA_Fb-gal-N3.txt TGA_FN2+.txt TGA_FNH2.txt TGA_Fb-gal.txt Standard curve onp and films functionality-Figure S2a.ods Protein liberation during use-Figure S2b.ods Equivalence test-Figure S3.ods Short description: Each file is a .ods, .txt, .xy or .csv file of each study/experiment