2020年11月11日 · In bromelain, the L-domain, residues 11–112 and 209–216 is mainly formed by α-helices while the R-domain, residues 2–10 and 113–208 has predominantly an antiparallel β-sheet structure ...

2018年11月15日 · The enzymes can be classified into seven categories including cysteine proteases which contain cysteine thiol in its catalytic triad or dyad. Cysteine proteases are broadly dispersed in nature. Some of the enzymes have been isolated from several plant kingdoms ( Arroyo-Reyna, Hernandez-Arana, & Arreguin-Espinosa, 1994 ).

Structure and biochemistry of bromelain. Bromelain is a protease that catalyzes proteolytic processes [12,20,27], and it is categorized as a cysteine proteinase (EC 3.4.22, CP, commonly known as thiol proteinase) because its active site has cysteine thiol [1,20].

Bromelain is also considered a thiol endopeptidase (internal clearing enzyme) [20], with the activity of all sulfhydryl endopeptidases depending upon the thiol group (SH) of a cysteine residue [3, 21]. Stem bromelain has a stable secondary structure and shows activity in the pH range 7–10, with its activity being irreversibly lost above pH 10 [22].

2018年11月15日 · The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain. The amino acid sequence and domain analysis of the fruit and stem bromelains demonstrated several differences and similarities of these cysteine protease family members.

Bromelain is an effective chemoresponsive proteolytic enzyme derived from pineapple stems. It contains several thiol endopeptidases and is extracted and purified via several methods. It is most commonly used as an anti-inflammatory agent, though scientists have also discovered its potential as an anticancer and antimicrobial agent.

2024年7月1日 · Bromelain is a complex mixture of thiol endopeptidases purified from the pineapple plant (Ananas comosus L) [94, 95]. Bromelain belongs to the group of proteases, classified as cysteine proteinase (EC 3.4.22, CP) due to the presence of the cysteine thiol in its active site [96]; it preferentially cleaves glycyl, alanyl and leucyl peptide bonds ...

2001年1月1日 · The spectral characteristics of stem bromelain suggest that this enzyme belongs to the alpha + beta protein class, as other cysteine proteinases do. In agreement with these results, quantitative estimation of secondary structures yielded amounts similar to those for papain and proteinase omega.

2021年7月27日 · Cysteine proteases (also called thiol proteases) are present in all living organisms and share a common catalytic mechanism involving a nucleophilic cysteine in the catalytic unit, which is composed of a triad of amino acids. The first isolated and characterized cysteine protease was papain obtained from papaya latex (Carica papaya). The enzyme ...

Bromelain is a protease enzyme derived from the stems of pineapples that is composed of a mixture of different thiol endopeptidases and other components like phosphatase, glucosidase, peroxidase, cellulase, escharase, and several protease inhibitors.