Literature DB >> 27770928

In situ chitin isolation from body parts of a centipede and lysozyme adsorption studies.

Esra Bulut1, Idris Sargin1, Ozlem Arslan2, Mehmet Odabasi2, Bahar Akyuz1, Murat Kaya3.   

Abstract

Isolation of structurally intact chitin samples for biotechnological applications has gained much recent attention. So far, three-dimensional chitin isolates have been obtained from only diplopods and sponges. In this study, three-dimensional chitin isolates were obtained from the body parts of centipede Scolopendra sp. (antennae, head, forcipule, collum, trunk, trunk legs and last pair of legs) without leading to structural failure. FT-IR spectra of chitin isolates confirmed that chitin samples are in α allomorph. TGA, XRD and SEM analyses and lysozyme adsorption studies revealed that each chitin isolate had different thermal stability, crystallinity and surface characteristics. Among the chitin isolates, Cu(II)-immobilized forcipule chitin showed the highest affinity for lysozyme (54.1mg/g), whereas chitin from last pair of legs exhibited the lowest affinity (3.7mg/g). This study demonstrated that structurally intact chitin isolates can be obtained from the body parts of centipede Scolopendra sp. (antennae, head, forcipule, collum, trunk, trunk legs and last pair of legs) by using a simple chemical procedure. Also, it gives a biotechnological perspective to the organisms in the group of Chilipoda.
Copyright © 2016 Elsevier B.V. All rights reserved.

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Keywords:  3-D chitin isolation; Biomaterial; Biopolymer; Metal immobilization; Protein adsorption

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Year:  2016        PMID: 27770928     DOI: 10.1016/j.msec.2016.08.048

Source DB:  PubMed          Journal:  Mater Sci Eng C Mater Biol Appl        ISSN: 0928-4931            Impact factor:   7.328


  1 in total

1.  α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors.

Authors:  Ömür Acet; Tülden İnanan; Burcu Önal Acet; Emrah Dikici; Mehmet Odabaşı
Journal:  Appl Biochem Biotechnol       Date:  2021-03-29       Impact factor: 2.926

  1 in total

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