Ethyl 2-benzyl-3-[3-(4-chloro-phen-yl)-1-phenyl-1H-pyrazol-4-yl]-4,6-dioxo-5-phenyl-octa-hydro-pyrrolo-[3,4-c]pyrrole-1-carboxyl-ate.

The title compound, C(37)H(31)ClN(4)O(4), crystallizes with two mol-ecules (A and B) in the asymmetric unit. The pyrrole rings in both mol-ecules are connected via cis fusion, whereas one ring has a twisted conformation and the other assumes a half-chair conformation. In the crystal, the A mol-ecules form inversion dimers via a pair of C-H⋯Cl inter-actions, while the B mol-ecules form chains propagating in [1[Formula: see text]0], via C-H⋯O inter-actions. In the crystal, there are also a number of C-H⋯π inter-actions present.

In situ immobilization of acid protease on mesoporous activated carbon packed column for the production of protein hydrolysates.

The mesoporous activated carbon (MAC) was used as a support material for in situ immobilization of acid protease (AP). The optimum temperature for the activities of both free and immobilized AP was found to be 50 degrees C. The catalytic efficiency of AP-MAC system has significantly been maintained for more than ten consecutive reaction cycles. The functional groups and surface morphology of the AP, MAC and AP-MAC were observed by Fourier transform infrared spectroscopy (FT-IR) and scanning electron microscopy (SEM). The production of protein hydrolysates was carried out from bovine serum albumin (BSA) using AP-MAC packed column and its properties were studied.

Acidogenic fermentation of proteinaceous solid waste and characterization of different bioconversion stages and extracellular products.

The purpose of this study was to investigate hydrolysis of animal fleshing (ANFL), a predominant tannery solid waste and to characterize the acetogenic fermentation products of anaerobic digestion. The acidogenic digestibility of the tannery solid wastes were evaluated up to 120 h using batch anaerobic digestion tests performed under mesophilic condition at 37 degrees C. The degradation of ANFL starts with non-fibrillar proteins and proceeds with fibrillar proteins. The release of aliphatic amino acid in the early stages of hydrolysis (24 h) and followed by aromatic amino acids (24-72 h) were evidenced by HPLC analysis. The maximum production of propionic and valeric acid were observed in 72 h followed by rapid increase in acetic acid in 96 h using GC-MS. Breakdown of ANFL and formations of other metabolites were evidenced by FT-IR and (1)H-NMR spectroscopy.