English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Genome sequence of  Serratia proteamaculans  568 revealed the presence of three family 33 chitin binding proteins (CBPs). The three  Sp  CBPs ( Sp  CBP21,  Sp  CBP28 and  Sp  CBP50) were heterologously expressed and purified.  Sp  CBP21 and  Sp  CBP50 showed binding preference to β-chitin, while  Sp  CBP28 did not bind to chitin and cellulose substrates. Both  Sp  CBP21 and  Sp  CBP50 were synergistic with four chitinases from  S. proteamaculans  568 ( Sp  ChiA,  Sp  ChiB,  Sp  ChiC and  Sp  ChiD) in degradation of α- and β-chitin, especially in the presence of external electron donor (reduced glutathione).  Sp  ChiD benefited most from  Sp  CBP21 or  Sp  CBP50 on α-chitin, while  Sp  ChiB and  Sp  ChiD had major advantage with these  Sp  CBPs on β-chitin. Dose responsive studies indicated that both the  Sp  CBPs exhibit synergism ≥0.2 µM. The addition of both  Sp  CBP21 and  Sp  CBP50 in different ratios to a synergistic mixture did not significantly increase the activity. Highly conserved polar residues, important in binding and activity of CBP21 from  S. marcescens  ( Sm  CBP21), were present in  Sp  CBP21 and  Sp  CBP50, while  Sp  CBP28 had only one such polar residue. The inability of  Sp  CBP28 to bind to the test substrates could be attributed to the absence of important polar residues.

Chitin Binding Proteins Act Synergistically with Chitinases in Serratia proteamaculans 568