What are the properties of Cellulase in supplements?

The properties of Cellulase

Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. Medically, Cellulase is used as a treatment for phytobezoars, a form of cellulose bezoar found in the human stomach, and it has exhibited efficacy in degrading polymicrobial bacterial biofilms by hydrolyzing the β(1-4) glycosidic linkages within the structural, matrix exopolysaccharides of the extracellular polymeric substance (EPS).



The supplements containing Cellulase


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Cellulase

TBS Ingredient ID (TBSI ID):
Name
Cellulase
Classification TypeIdentifier
CAS:
A proprietary registry number assigned by the Chemical Abstracts Service (CAS) division of the American Chemical Society (ACS)
9012-54-8
NIST:
The National Institute of Standards and Technology (NIST)
ChemIDplus:
United States National Library of Medicine - TOXNET (Toxicology Data Network).
EC Number:
A seven-digit regulatory identifier currently assigned by the European Chemicals Agency (ECHA) known as a European Community (EC) number
3.2.1.4
Pfam:
The Pfam database is a large collection of protein families, each represented by multiple sequence alignments and hidden Markov models (HMMs)
InterPro:
InterPro - Protein sequence analysis & classification
PROSITE:
Database of protein domains, families and functional sites
SCOP:
The Structural Classification of Proteins (SCOP) database is a largely manual classification of protein structural domains based on similarities of their structures and amino acid sequences
SUPERFAMILY:
SUPERFAMILY is a database of structural and functional annotation for all proteins and genomes
CDD:
The Conserved Domains and Protein Classification (CDD) is a protein annotation resource that consists of a collection of well-annotated multiple sequence alignment models for ancient domains and full-length proteins