Synthesis of Glycinamides Using Protease Immobilized Magnetic Nanoparticles

Overview

Journal Biotechnol Rep (Amst)

Specialty Biotechnology

Date 2017 Mar 30

PMID 28352550

Citations 5

Authors

Abha Sahu

Pallavi Sharad Badhe

Ravindra Adivarekar

Mayur Ramrao Ladole

Aniruddha Bhalchandra Pandit

Affiliations

Soon will be listed here.

Abstract

In the present investigation, was isolated from slaughterhouse waste and screened for the production of protease enzyme. The purified protease was successfully immobilized on magnetic nanoparticles (MNPs) and used for the synthesis of series of glycinamides. The binding and thermal stability of protease on MNPs was confirmed by FTIR spectroscopy and TGA analysis. The surface morphology of MNPs before and after protease immobilization was carried out using SEM analysis. XRD pattern revealed no phase change in MNPs after enzyme immobilization. The processing parameters for glycinamides synthesis viz. temperature, pH, and time were optimized using Response Surface Methodology (RSM) by using Design Expert (9.0.6.2). The maximum yield of various amides 2 butyramidoacetic acid (AMD-1,83.4%), 2-benzamidoacetic acid (AMD-2,80.5%) and 2,2'((carboxymethyl) amino)-2-oxoethyl)-2-hydroxysuccinyl)bis(azanediyl))diacetic acid (AMD-3,80.8%) formed was observed at pH-8, 50 °C and 30 min. The synthesized immobilized protease retained 70% of the initial activity even after 8 cycles of reuse.

Citing Articles

Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications.

Gama Cavalcante A, Nascimento Dari D, da Silva Aires F, Carlos de Castro E, Dos Santos K, Sousa Dos Santos J RSC Adv. 2024; 14(25):17946-17988.

PMID: 38841394 PMC: 11151160. DOI: 10.1039/d4ra02939a.

Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test.

Alici E, Arabaci G Glob Chall. 2024; 8(1):2300102.

PMID: 38223888 PMC: 10784196. DOI: 10.1002/gch2.202300102.

Immobilization of α-transglucosidase on silica-coated magnetic nanoparticles and its application for production of isomaltooligosaccharide from the potato peel.

Maurya R, Ali U, Kaul S, Bhaiyya R, Singh R, Mazumder K Sci Rep. 2023; 13(1):12708.

PMID: 37543692 PMC: 10404235. DOI: 10.1038/s41598-023-38266-8.

Magnetite Nanoparticles Functionalized with RNases against Intracellular Infection of .

Rangel-Munoz N, Suarez-Arnedo A, Anguita R, Prats-Ejarque G, Osma J, Munoz-Camargo C Pharmaceutics. 2020; 12(7).

PMID: 32640506 PMC: 7408537. DOI: 10.3390/pharmaceutics12070631.

Optimization of pectinase-assisted and tri-solvent-mediated extraction and recovery of lycopene from waste tomato peels.

Munde P, Muley A, Ladole M, Pawar A, Talib M, Parate V 3 Biotech. 2017; 7(3):206.

PMID: 28667641 PMC: 5493572. DOI: 10.1007/s13205-017-0825-3.

References

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

Talekar S, Ghodake V, Ghotage T, Rathod P, Deshmukh P, Nadar S . Novel magnetic cross-linked enzyme aggregates (magnetic CLEAs) of alpha amylase. Bioresour Technol. 2012; 123:542-7. DOI: 10.1016/j.biortech.2012.07.044. View

Elchinger P, Delattre C, Faure S, Roy O, Badel S, Bernardi T . Immobilization of proteases on chitosan for the development of films with anti-biofilm properties. Int J Biol Macromol. 2014; 72:1063-8. DOI: 10.1016/j.ijbiomac.2014.09.061. View

Bordusa F . Nonconventional amide bond formation catalysis: programming enzyme specificity with substrate mimetics. Braz J Med Biol Res. 2000; 33(5):469-85. DOI: 10.1590/s0100-879x2000000500001. View

Ren Y, Rivera J, He L, Kulkarni H, Lee D, Messersmith P . Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating. BMC Biotechnol. 2011; 11:63. PMC: 3212977. DOI: 10.1186/1472-6750-11-63. View

Yazawa K, Numata K . Recent advances in chemoenzymatic peptide syntheses. Molecules. 2014; 19(9):13755-74. PMC: 6271809. DOI: 10.3390/molecules190913755. View

Pal A, Khanum F . Efficacy of xylanase purified from Aspergillus niger DFR-5 alone and in combination with pectinase and cellulase to improve yield and clarity of pineapple juice. J Food Sci Technol. 2013; 48(5):560-8. PMC: 3551128. DOI: 10.1007/s13197-010-0175-1. View

Nadar S, Muley A, Ladole M, Joshi P . Macromolecular cross-linked enzyme aggregates (M-CLEAs) of α-amylase. Int J Biol Macromol. 2015; 84:69-78. DOI: 10.1016/j.ijbiomac.2015.11.082. View

Ulijn R, Baragana B, Halling P, Flitsch S . Protease-catalyzed peptide synthesis on solid support. J Am Chem Soc. 2002; 124(37):10988-9. DOI: 10.1021/ja026912d. View

10.

Abdul Halim S, Kamaruddin A, Fernando W . Continuous biosynthesis of biodiesel from waste cooking palm oil in a packed bed reactor: optimization using response surface methodology (RSM) and mass transfer studies. Bioresour Technol. 2008; 100(2):710-6. DOI: 10.1016/j.biortech.2008.07.031. View

11.

Toplak A, Nuijens T, Quaedflieg P, Wu B, Janssen D . Peptide synthesis in neat organic solvents with novel thermostable proteases. Enzyme Microb Technol. 2015; 73-74:20-8. DOI: 10.1016/j.enzmictec.2015.03.003. View

12.

GAERTNER H, Puigserver A . Kinetics and specificity of serine proteases in peptide synthesis catalyzed in organic solvents. Eur J Biochem. 1989; 181(1):207-13. DOI: 10.1111/j.1432-1033.1989.tb14712.x. View

13.

Talekar S, Pandharbale A, Ladole M, Nadar S, Mulla M, Japhalekar K . Carrier free co-immobilization of alpha amylase, glucoamylase and pullulanase as combined cross-linked enzyme aggregates (combi-CLEAs): a tri-enzyme biocatalyst with one pot starch hydrolytic activity. Bioresour Technol. 2013; 147:269-275. DOI: 10.1016/j.biortech.2013.08.035. View

14.

Delattre C, Pierre G, Gardarin C, Traikia M, Elboutachfaiti R, Isogai A . Antioxidant activities of a polyglucuronic acid sodium salt obtained from TEMPO-mediated oxidation of xanthan. Carbohydr Polym. 2014; 116:34-41. DOI: 10.1016/j.carbpol.2014.04.054. View