Bioresource Technology 2009-02-01

Biodegradation of high molecular weight lignin under sulfate reducing conditions: lignin degradability and degradation by-products.

Jae-Jung Ko, Yoshihisa Shimizu, Kazuhiro Ikeda, Seog-Ku Kim, Chul-Hwi Park, Saburo Matsui

Index: Bioresour. Technol. 100 , 1622-1627, (2009)

Full Text: HTML

Abstract

This study is designed to investigate the biodegradation of high molecular weight (HMW) lignin under sulfate reducing conditions. With a continuously mesophilic operated reactor in the presence of co-substrates of cellulose, the changes in HMW lignin concentration and chemical structure were analyzed. The acid precipitable polymeric lignin (APPL) and lignin monomers, which are known as degradation by-products, were isolated and detected. The results showed that HMW lignin decreased and showed a maximum degradation capacity of 3.49 mg/l/day. APPL was confirmed as a polymeric degradation by-product and was accumulated in accordance with HMW lignin reduction. We also observed non-linear accumulation of aromatic lignin monomers such as hydrocinnamic acid. Through our experimental results, it was determined that HMW lignin, when provided with a co-substrate of cellulose, is biodegraded through production of APPL and aromatic monomers under anaerobic sulfate reducing conditions with a co-substrate of cellulose.


Related Compounds

Related Articles:

RNAi-mediated suppression of p-coumaroyl-CoA 3'-hydroxylase in hybrid poplar impacts lignin deposition and soluble secondary metabolism.

2008-03-18

[Proc. Natl. Acad. Sci. U. S. A. 105 , 4501-4506, (2008)]

Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth and development in Arabidopsis.

2009-12-01

[Plant J. 60 , 771-782, (2009)]

A simple method to determine trypsin and chymotrypsin inhibitory activity.

2004-06-30

[J. Biochem. Biophys. Methods 59 , 241-251, (2004)]

Ribosomal binding and dipeptide formation by misacylated tRNA(Phe),S.

1988-09-20

[Biochemistry 27 , 7254-7262, (1988)]

Chemotactic activity from rabbit peritoneal neutrophils. Lack of identity with N-acetyl-DL-phenylalanine beta-napthyl esterase.

1976-08-12

[Biochim. Biophys. Acta 445 , 112-117, (1976)]

More Articles...