Collagen and collagenolytic proteases: A review

2018 ◽  
Vol 15 ◽  
pp. 43-55 ◽  
Author(s):  
Prashant K. Bhagwat ◽  
Padma B. Dandge
Keyword(s):  
Collagenolytic Proteases

Maturation process and characterization of a novel thermostable and halotolerant subtilisin-like protease with high collagenolytic but low gelatinolytic activity

2021 ◽  
Author(s):  
Kui Zhang ◽  
Qianqian Huang ◽  
Yu Li ◽  
Lanhua Liu ◽  
Xiao-Feng Tang ◽  
...  
Keyword(s):  
High Temperatures ◽  
Type I Collagen ◽  
Elevated Temperatures ◽  
Catalytic Domain ◽  
Ion Pairs ◽  
Gelatinolytic Activity ◽  
Type I ◽  
Fish Scale ◽  
Collagenolytic Proteases ◽  
Collagenolytic Protease

Enzymatic degradation of collagen is of great industrial and environmental significance; however, little is known about thermophile-derived collagenolytic proteases. Here, we report a novel collagenolytic protease (TSS) from thermophilic Brevibacillus sp. WF146. The TSS precursor comprises a signal peptide, an N-terminal propeptide, a subtilisin-like catalytic domain, a β-jelly roll (βJR) domain, and a prepeptidase C-terminal (PPC) domain. The maturation of TSS involves a stepwise autoprocessing of the N-terminal propeptide and the PPC domain, and the βJR rather than the PPC domain is necessary for correct folding of the enzyme. Purified mature TSS displayed optimal activity at 70°C and pH 9.0, a half-life of 1.5 h at 75°C, and an increased thermostability with rising salinity up to 4 M. TSS possesses an increased number of surface acidic residues and ion pairs, as well as four Ca 2+ -binding sites, which contribute to its high thermostability and halotolerance. At high temperatures, TSS exhibited high activity toward insoluble type I collagen and azocoll, but showed a low gelatinolytic activity, with a strong preference for Arg and Gly at the P1 and P1’ positions, respectively. Both the βJR and PPC domains could bind but not swell collagen, and thus facilitate TSS-mediated collagenolysis via improving the accessibility of the enzyme to the substrate. Additionally, TSS has the ability to efficiently degrade fish scale collagen at high temperatures. IMPORTANCE Proteolytic degradation of collagen at high temperatures has the advantages of increasing degradation efficiency and minimizing the risk of microbial contamination. Reports on thermostable collagenolytic proteases are limited, and their maturation and catalytic mechanisms remain to be elucidated. Our results demonstrate that the thermophile-derived TSS matures in an autocatalytic manner, and represents one of the most thermostable collagenolytic proteases reported so far. At elevated temperatures, TSS prefers hydrolyzing insoluble heat-denatured collagen rather than gelatin, providing new insight into the mechanism of collagen degradation by thermostable collagenolytic proteases. Moreover, TSS has the potential to be used in recycling collagen-rich wastes such as fish scales.

Purification and Characterization of Collagenolytic Proteases from the Hepatopancreas of Northern Shrimp (Pandalus eous)

2003 ◽  
Vol 51 (3) ◽  
pp. 777-783 ◽  
Author(s):  
Hitoshi Aoki ◽  
Md. Nazmul Ahsan ◽  
Kenji Matsuo ◽  
Toshihiko Hagiwara ◽  
Shugo Watabe
Keyword(s):  
Purification And Characterization ◽  
Collagenolytic Proteases ◽  
Northern Shrimp

Substrate specificity of collagenolytic proteases from the king crab Paralithodes camtschatica

1994 ◽  
Vol 107 (3) ◽  
pp. 411-417 ◽  
Author(s):  
Ivan Yu. Sakharov ◽  
Fedor E. Litvin ◽  
Olga V. Mitkevitch ◽  
Gennady P. Samokhin ◽  
Zhanna D. Bespalova
Keyword(s):  
Substrate Specificity ◽  
King Crab ◽  
Collagenolytic Proteases ◽  
Paralithodes Camtschatica

Application of bacterial collagenolytic proteases for the extraction of type I collagen from the skin of bigeye tuna (Thunnus obesus)

LWT ◽  
2018 ◽  
Vol 89 ◽  
pp. 44-51 ◽  
Author(s):  
Raju Ahmed ◽  
Adane Tilahun Getachew ◽  
Yeon-Jin Cho ◽  
Byung-Soo Chun
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Bigeye Tuna ◽  
Collagenolytic Proteases ◽  
Thunnus Obesus

The isolation and properties of collagenolytic proteases from crab hepatopancreas

1990 ◽  
Vol 166 (3) ◽  
pp. 1411-1420 ◽  
Author(s):  
O.A. Klimova ◽  
S.I. Borukhov ◽  
N.I. Solovyeva ◽  
T.O. Balaevskaya ◽  
A.Ya. Strongin
Keyword(s):  
Collagenolytic Proteases ◽  
Crab Hepatopancreas

Box–Behnken analysis and storage of spray-dried collagenolytic proteases from Myceliophthora thermophila submerged bioprocess

2017 ◽  
Vol 47 (5) ◽  
pp. 473-480 ◽  
Author(s):  
Youssef Ali Abou Hamin Neto ◽  
Luciana Barbosa Coitinho ◽  
Luis Alexandre Pedro de Freitas ◽  
Hamilton Cabral
Keyword(s):  
Myceliophthora Thermophila ◽  
Collagenolytic Proteases ◽  
And Storage ◽  
Spray Dried
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