Alginate/protamine/silica hybrid capsules with ultrathin membranes for laccase immobilization

Research output: Contribution to journalArticlepeer-review

Standard

Alginate/protamine/silica hybrid capsules with ultrathin membranes for laccase immobilization. / Wang, Ji Yun; Yu, Hai Rong; Xie, Rui; Ju, Xiao Jie; Yu, Ya Lan; Chu, Liang Yin; Zhang, Zhibing.

In: AIChE Journal, Vol. 59, No. 2, 02.2013, p. 380-389.

Research output: Contribution to journalArticlepeer-review

Harvard

APA

Vancouver

Author

Wang, Ji Yun ; Yu, Hai Rong ; Xie, Rui ; Ju, Xiao Jie ; Yu, Ya Lan ; Chu, Liang Yin ; Zhang, Zhibing. / Alginate/protamine/silica hybrid capsules with ultrathin membranes for laccase immobilization. In: AIChE Journal. 2013 ; Vol. 59, No. 2. pp. 380-389.

Bibtex

@article{6782e2ebaca14b48bdb982080ea7366c,
title = "Alginate/protamine/silica hybrid capsules with ultrathin membranes for laccase immobilization",
abstract = "A novel type of core-shell capsules with ultrathin alginate/protamine/silica (APSi) hybrid membranes are successfully fabricated through a coextrusion minifluidic approach and a biosilicification method for immobilization of laccase. The ultrathin membranes were beneficial to the mass transfer across the capsule membranes, and the silica layer on the outer surface was efficient to inhibit the swelling of the capsule membranes. The immobilizing yield was considered to be 100% because all the enzyme molecules were encapsulated inside the capsules through the proposed method, and the laccase activity immobilized in APSi capsules was 61.8 mmol·g-1·min-1. The thermal, pH and storage stabilities of the immobilized laccase in APSi capsules were determined in comparison with free laccase. The stability of encapsulated laccase was significantly improved, which was as high as 67% after 20 days. The residual relative activity of encapsulated laccase remained 45% after 10 cycles.",
keywords = "Alginate/protamine/silica hybrid capsules, Biomimetic capsules, Enzyme immobilization, Laccase, Silicification",
author = "Wang, {Ji Yun} and Yu, {Hai Rong} and Rui Xie and Ju, {Xiao Jie} and Yu, {Ya Lan} and Chu, {Liang Yin} and Zhibing Zhang",
year = "2013",
month = feb,
doi = "10.1002/aic.13834",
language = "English",
volume = "59",
pages = "380--389",
journal = "AIChE Journal",
issn = "0001-1541",
publisher = "Wiley",
number = "2",

}

RIS

TY - JOUR

T1 - Alginate/protamine/silica hybrid capsules with ultrathin membranes for laccase immobilization

AU - Wang, Ji Yun

AU - Yu, Hai Rong

AU - Xie, Rui

AU - Ju, Xiao Jie

AU - Yu, Ya Lan

AU - Chu, Liang Yin

AU - Zhang, Zhibing

PY - 2013/2

Y1 - 2013/2

N2 - A novel type of core-shell capsules with ultrathin alginate/protamine/silica (APSi) hybrid membranes are successfully fabricated through a coextrusion minifluidic approach and a biosilicification method for immobilization of laccase. The ultrathin membranes were beneficial to the mass transfer across the capsule membranes, and the silica layer on the outer surface was efficient to inhibit the swelling of the capsule membranes. The immobilizing yield was considered to be 100% because all the enzyme molecules were encapsulated inside the capsules through the proposed method, and the laccase activity immobilized in APSi capsules was 61.8 mmol·g-1·min-1. The thermal, pH and storage stabilities of the immobilized laccase in APSi capsules were determined in comparison with free laccase. The stability of encapsulated laccase was significantly improved, which was as high as 67% after 20 days. The residual relative activity of encapsulated laccase remained 45% after 10 cycles.

AB - A novel type of core-shell capsules with ultrathin alginate/protamine/silica (APSi) hybrid membranes are successfully fabricated through a coextrusion minifluidic approach and a biosilicification method for immobilization of laccase. The ultrathin membranes were beneficial to the mass transfer across the capsule membranes, and the silica layer on the outer surface was efficient to inhibit the swelling of the capsule membranes. The immobilizing yield was considered to be 100% because all the enzyme molecules were encapsulated inside the capsules through the proposed method, and the laccase activity immobilized in APSi capsules was 61.8 mmol·g-1·min-1. The thermal, pH and storage stabilities of the immobilized laccase in APSi capsules were determined in comparison with free laccase. The stability of encapsulated laccase was significantly improved, which was as high as 67% after 20 days. The residual relative activity of encapsulated laccase remained 45% after 10 cycles.

KW - Alginate/protamine/silica hybrid capsules

KW - Biomimetic capsules

KW - Enzyme immobilization

KW - Laccase

KW - Silicification

UR - http://www.scopus.com/inward/record.url?scp=84872868543&partnerID=8YFLogxK

U2 - 10.1002/aic.13834

DO - 10.1002/aic.13834

M3 - Article

AN - SCOPUS:84872868543

VL - 59

SP - 380

EP - 389

JO - AIChE Journal

JF - AIChE Journal

SN - 0001-1541

IS - 2

ER -